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  • Anti-cancer activity of di- and tri-organotin(IV) compounds with D-(+)-Galacturonic acid on human tumor cells
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-09
    Alessandro Attanzio, Maristella Ippolito, Maria Assunta Girasolo, Filippo Saiano, Archimede Rotondo, Simona Rubino, Luigi Mondello, Massimo L. Capobianco, Piera Sabatino, Luisa Tesoriere, Girolamo Casella

    We have compared the anti-proliferative activity in vitro, of R2SnGala (1-3) [R = Me, n-Bu, Ph] and novel R3SnGala (4, 5) [R = Me, n-Bu] with D-(+)-Galacturonic acid [HGala; Galaq-, q = (2) and (1) for R2SnGala and R3SnGala, respectively] compounds, towards human tumor cell lines of intestinal carcinoma (HCT-116) and breast adenocarcinoma (MCF-7). The new synthesized 4 and 5 compounds were characterized, in solution, by 1H, 13C and 119Sn NMR, that showed that HGala acts as monoanionic moiety and evidenced the dynamic behavior of the compounds, due to inter-conversions involving the anomeric carbon atom of the ligand. Cell viability, apoptosis induction and cell cycle distribution were analyzed by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) colorimetric assay and flow cytometry, respectively. The cytotoxicity of the compounds, in the micro-submicromolar range, changed in the order of the organotin(IV) moieties, according to 5 > 3 > 2, while 1 and 4, containing MenSn(IV) (n = 2,3) moieties, were ineffective. Compound 5 showed peculiar cytotoxic effects. It did not cause time dependent inhibition of cell growth nor accumulated into the cells. Cell death induced by the active 2, 3, and 5, was shown to be apoptotic by measuring the exposure of phosphatidylserine to the outer membrane and the loss of mitochondrial potential. All the cytotoxic compounds induced an accumulation of cells in the subG0/G1phase, while only 2 and 3 perturbed the cell cycle confining viable cells in G0/G1phase. Finally, none of the compounds investigated affected the viability of normal intestinal or liver cells, indicating selectivity towards tumor cells.

  • A stable zinc(II)-mediated base pair in a parallel-stranded DNA duplex
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-07-05
    Biswarup Jash, Jens Müller

    A stable zinc(II)-mediated base pair was formed within a parallel-stranded DNA duplex comprising a GNA (glycol nucleic acid) functionalized nucleoside analog containing the artificial nucleobase 1H-imidazo[4,5-f][1,10]phenanthroline (P). The formation of the metal-mediated base pair was confirmed by UV and CD spectroscopic analyses. In the Zn(II)-mediated homo base pairs of the type P–Zn(II)–P, the metal ion adopts a [2 + 2] coordination environment. CD spectroscopic data suggest that the chiral metal complex is formed enantiospecifically, likely induced by the helical chirality of the surrounding DNA duplex. The Zn(II)-mediated base pair stabilizes the DNA oligonucleotide duplex by 9 °C. This stable Zn(II)-mediated base pair within a parallel-stranded duplex extends the scope of site-specific functionalization of nucleic acids by virtue of metal-mediated base pairing.

  • Pro-apoptotic activity of ruthenium 1-methylimidazole complex on non-small cell lung cancer
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-07-04
    Júlia Scaff Moreira Dias, Henrique Vieira Reis Silva, Guilherme Álvaro Ferreira da Silva, Marisa Ionta, Charlane Cimini Corrêa, Fernando Almeida, Legna Colina-Vegas, Marília Imaculada Frazão Barbosa, Antônio Carlos Doriguetto

    Herein, novel ruthenium(II) complexes containing 1-methylimidazole as a ligand were obtained with the following formulas: [RuCl(1Meim)(dppb)(bpy)]Cl (1), [RuCl(1Meim)(dppb)(4,4′-DMbpy)]Cl (2), [RuCl(1Meim)(dppb)(5,5′-DMbpy)]Cl (3) and [RuCl(1Meim)(dppb)(phen)]Cl (4) where, 1Meim = 1-methylimidazole, dppb = 1,4-Bis(diphenylphosphino)butane, bpy = 2,2′-bipyridine, 4,4′-DMbpy = 4,4′-dimethyl-2,2′-bipyridine, 5,5′-DMbpy = 5,5′-dimethyl-2,2′-bipyridine and phen = 1,10-phenanthroline. Additionally, crystal structures containing the cations of (1) and (3) were obtained when the counter ion was exchanged, leading to the formation of [RuCl(1Meim)(dppb)(bpy)]PF6 (5) and [RuCl(1Meim)(dppb)(5,5′-DMbpy)]PF6 methanol solvate (6) where PF6 = hexafluorophosphate, showing one 1-methylimidazole molecule coordinated through the imidazole nitrogen, as expected. The complexes were characterized by elemental analysis, molar conductivity, infrared and UV–Vis spectroscopy, 1H, 13C{1H} and 31P{1H} NMR, mass spectrometry and cyclic voltammetry. The interactions of complexes 1–4 with DNA and human serum albumin (HSA) were evaluated, and the cytotoxicity profiles of compounds 1–4 were determined using four different tumor cell lines derived from human cancers (melanoma: HT-144, colon: HCT-9, breast: MDA-MB-231 and lung: A549). A higher cytotoxic activity was observed for compound (3) against non-small cell lung cancer (A549). Complex (3) inhibited the clonogenic capacity and cell cycle progression of A549 cells and induced apoptosis involving mitochondrial pathway activation. Therefore, the data obtained in the present study support further investigations concerning molecular targets of complex (3) in non-small cell lung cancer.

  • Magnetic nanoparticles as a support for a copper (II) complex with nuclease activity
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-06-30
    Maria A.S. Silva, Adolfo I.B. Romo, Dieric S. Abreu, Marta S.P. Carepo, Luis Lemus, Miguel Jafelicci Jr, Tércio F. Paulo, Otaciro R. Nascimento, Esteban Vargas, Juliano C. Denardin, Izaura C.N. Diógenes
  • Coordination capacity of cytosine, adenine and derivatives towards open-paddlewheel diruthenium compounds
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-06-30
    Ángela Valentín-Pérez, Josefina Perles, Santiago Herrero, Reyes Jiménez-Aparicio
  • Cytotoxicity, dual-targeting apoptosis induction evaluation of multinuclear cu complexes based on pyrazine-benzimidazole derivative
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-06-30
    Jiyong Hu, Shufang Chen, Ruina Mao, Chunli Liao, Hao Yang, Jin'an Zhao
  • MicroRNA-193b-3p regulates hepatocyte apoptosis in selenium-deficient broilers by targeting MAML1 ☆
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-06-28
    Tianqi Liu, Tianshu Yang, Zhe Xu, Siran Tan, Tingru Pan, Na Wan, Shu Li
  • Synthesis and characterization of a flexibility fluorescent magnetic Fe3O4@SiO2/CdTe-NH2 nanoprobe
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-06-15
    Min Wang, Xiaofang Fei, Shaowu Lv, Ye Sheng, Haifeng Zou, Yanhua Song, Fei Yan, Qianlong Zhu, Keyan Zheng
  • 更新日期:2018-06-15
  • Future perception in P450 research
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-06-07
    Tsuneo Omura
  • Cross-linked cytochrome P450 BM3 aggregates promoted by Ru(II)-diimine complexes bearing aldehyde groups
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-06-05
    Minh Quan Do, Evelynn Henry, Mallory Kato, Lionel Cheruzel
  • Bifunctional 3-hydroxy-4-pyridinones as effective aluminium chelators: Synthesis, solution equilibrium studies and in vivo evaluation
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-30
    Anna Irto, Paola Cardiano, Karam Chand, Rosalia Maria Cigala, Francesco Crea, Concetta De Stefano, Lurdes Gano, Silvio Sammartano, Maria Amélia Santos
  • The role of ancillary ligand substituents in the biological activity of triruthenium-NO complexes
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-30
    Camila Fontes Neves da Silva, Bruna Possato, Lilian Pereira Franco, Loyanne Carla Barbosa Ramos, Sofia Nikolaou
  • Determining the glycation site specificity of human holo-transferrin
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-26
    André M.N. Silva, João T.S. Coimbra, Maria M. Castro, Ângela Oliveira, Natércia F. Brás, Pedro A. Fernandes, Maria J. Ramos, Maria Rangel
  • The trans-[Ru(PPh3)2(N,N-dimethyl-N′-thiophenylthioureato-k2O,S)(bipy)]PF6 complex has pro-apoptotic effects on triple negative breast cancer cells and presents low toxicity in vivo
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-24
    Amanda Blanque Becceneri, Cecília Patrícia Popolin, Ana Maria Plutin, Edson Luis Maistro, Eduardo Ernesto Castellano, Alzir Azevedo Batista, Márcia Regina Cominetti
  • 更新日期:2018-05-24
  • 更新日期:2018-05-24
  • Interaction of 17α-hydroxylase, 17(20)-lyase (CYP17A1) inhibitors – abiraterone and galeterone – with human sterol 14α-demethylase (CYP51A1) ☆
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-21
    Rami Masamrekh, Alexey Kuzikov, Alexander Veselovsky, Iliya Toropygin, Tatsiana Shkel, Natalia Strushkevich, Andrey Gilep, Sergey Usanov, Alexander Archakov, Victoria Shumyantseva
  • Functional modeling of the MnCAT active site with a dimanganese(III) complex of an unsymmetrical polydentate N3O3 ligand
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-18
    Gabriela N. Ledesma, Elodie Anxolabéhère-Mallart, Laurent Sabater, Christelle Hureau, Sandra R. Signorella
  • Collagen promotes matrix vesicle-mediated mineralization by vascular smooth muscle cells
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-18
    Monika Roszkowska, Agnieszka Strzelecka-Kiliszek, Laurence Bessueille, René Buchet, David Magne, Slawomir Pikula
  • 更新日期:2018-05-18
  • Investigating the target organs of novel anti-diabetic zinc complexes with organo‑selenium ligands
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-12
    Takayuki Nishiguchi, Yutaka Yoshikawa, Hiroyuki Yasui
  • Cationic Au(I) complexes with aryl-benzothiazoles and their antibacterial activity
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-11
    Jenny Stenger-Smith, Indranil Chakraborty, Pradip K. Mascharak
  • 更新日期:2018-05-11
  • Effects on estrogen-dependent and triple negative breast cancer cells growth of Ni(II), Zn(II) and Cd(II) complexes with the Schiff base derived from pyridine-2-carboxaldehyde and 5,6-diamino-1,3-dimethyluracil explored through the renin-angiotensin system (RAS)-regulating aminopeptidases
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-09
    Nuria A. Illán-Cabeza, Sonia B. Jiménez-Pulido, Francisco Hueso-Ureña, Ma Jesús Ramírez-Expósito, Purificación Sánchez-Sánchez, José M. Martínez-Martos, Miguel N. Moreno-Carretero
  • Investigating Cytochrome P450 specificity during glycopeptide antibiotic biosynthesis through a homologue hybridization approach
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-03
    Clara Brieke, Miroslaw Tarnawski, Anja Greule, Max J. Cryle

    Cytochrome P450 enzymes perform an impressive range of oxidation reactions against diverse substrate scaffolds whilst generally maintaining a conserved tertiary structure and active site chemistry. Within secondary metabolism, P450 enzymes play widespread and important roles in performing crucial modifications of precursor molecules, with one example of the importance of such reactions being found in the biosynthesis of the glycopeptide antibiotics (GPAs). In GPA biosynthesis P450s, known as Oxy enzymes, are key players in the cyclization of the linear GPA peptide precursor, which is a process that is both essential for their antibiotic activity and is the source of the synthetic challenge of these important antibiotics. In this work, we developed chimeric P450 enzymes from GPA biosynthesis based on two homologues from different GPA biosynthesis pathways – vancomycin and teicoplanin – as an approach to explore the divergent catalytic behavior of the two parental homologues. We could generate, crystalize and explore the activity of new hybrid P450 enzymes from GPA biosynthesis and show that the unusual in vitro behavior of the vancomycin OxyB homologue does not stem from the major regions of the P450 active site, and that additional regions in and around the P450 active site must contribute to the unusual properties of this P450 enzyme. Our results further show that it is possible to successfully transplant entire regions of secondary structure between such P450s and retain P450 expression and activity, which opens the door to use such targeted approaches to generate and explore novel biosynthetic P450 enzymes.

  • Structural stabilities of calcium proteins: Human intelectin-1 and frog lectin XEEL
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-02
    John J. Kozak, Harry B. Gray, Roberto A. Garza-López, Kittikhun Wangkanont

    We extend our study of the structural stability of helical and nonhelical regions in chain A of human intelectin-1 to include a second human intelectin (4WMY) and the frog protein “Xenopus embryonic epidermal lectin” (XEEL). These unique lectins have been shown to recognize carbohydrate residues found exclusively in microbes, thus they could potentially be developed into novel microbe detection and sequestration tools. We believe that by studying the structural stability of these proteins we can provide insights on their biological role and activities. Using a geometrical model introduced previously, we perform computational analyses of protein crystal structures that quantify the resiliency of the native state to steric perturbations. Based on these analyses, we conclude that differences in the resiliency of the human and frog proteins can be attributed primarily to differences in non-helical regions and to residues near Ca ions. Since these differences are particularly pronounced in the vicinity of the ligand binding site, they provide an explanation for the finding that human intelectin-1 has a higher affinity for a ligand than XEEL. We also present data on conserved and position-equivalent pairs of residues in 4WMY and XEEL. We identify residue pairs as well as regions in which the influence of neighboring residues is nearly uniform as the parent protein denatures. Since the structural signatures are conserved, this identification provides a basis for understanding why both proteins exhibit trimeric structures despite poor sequence conservation at the interface.

  • Comparative assessment of metal-specific adipogenic activity in zinc and vanadium-citrates through associated gene expression
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-05-01
    O. Tsave, M.P. Yavropoulou, M. Kafantari, C. Gabriel, J.G. Yovos, A. Salifoglou

    Diabetes mellitus comprises a group of metabolic abnormalities due to insulin deficiency and/or resistance. Obesity contributes to diabetes, with a strong causal relationship existing between diabetes and insulin resistance, especially in patients with Diabetes mellitus II. Adipocytes emerge as key constituents of adipose tissue physiology. In their pre-mature form to mature state transformation, adipocytes fully exemplify one of the key adipogenic actions of insulin. Poised to a) gain insight into adipogenesis leading to antidiabetic factors, and b) investigate adipogenesis through careful examination of insulin contributions to interwoven mechanistic pathways, a systematic comparative study was launched involving well-defined metal-citrates (zinc and vanadium), the chemical reactivity of which was in line with their chemistry under physiological conditions. Selection of the specific compounds was based on their common aqueous coordination chemistry involving the physiological chelator citric acid. Cellular maturation of pre-adipocytes to their mature form was pursued in the presence-absence of insulin and employment of closely linked genetic targets, key to adipocyte maturation (Peroxisome proliferator-activated receptor gamma (PPAR-γ), Glucose transporter 1,3,4 (GLUT 1,3,4), Adiponectin (ADIPOQ), Glucokinase (GCK), and Insulin receptor (INS-R)). The results show a) distinct adipogenic biological profiles for the metalloforms involved in a dose-, time- and nature-dependent manner, and b) metal ion-specific adipogenic response-signals at the same or higher level than insulin toward all selected targets. Collectively, the foundations have been established for future exploitation of the distinct metal-specific adipogenic factors contributing to the functional maturation of adipose tissue and their use toward hyperglycemic control in Diabetes mellitus.

  • Heterodinuclear Zn(II)−Fe(III) and Homodinuclear M(II)−M(II) [M = Zn and Ni] complexes of a Bicompartmental [N6O] ligand as synthetic mimics of the hydrolase family of enzymes
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-30
    Chandni Pathak, Dharmendra Kumar, Manoj Kumar Gangwar, Darshan Mhatre, Thierry Roisnel, Prasenjit Ghosh

    Heterodinuclear mixed valence [Zn(II)−Fe(III)] and the homodinuclear [Zn(II)−Zn(II)] and [Ni(II)−Ni(II)] complexes of a bicompartmental ligand containing a bridging phenoxy as a O−donor and four pyridyl moieties and two amine moieties as the N−donors exhibit phosphoester hydrolysis activity similar to the hydrolase family of enzymes. While the heterodinuclear [Zn(II)−Fe(III)] (2) complex was obtained by the sequential addition of Fe(NO3)3∙9H2O and Zn(OAc)2∙2H2O to the ligand 2,6‑bis{[bis(2‑pyridylmethyl)amino]methyl}‑4‑t‑butylphenol (HL) (1) in moderate yield of 37%, the homodinuclear [Zn(II)−Zn(II)] (3) and [Ni(II)−Ni(II)] (4) complexes were obtained by the direct reaction of the ligand (1) with Zn(OAc)2∙2H2O and Ni(OAc)2∙2H2O respectively, in good to moderate yields (43–63%). Based on the spectrophotometric titration and the mass spectrometry studies, a monoaquated and dihydroxo species 2C, 3C and 4C has been identified as the catalytically active species responsible for the phosphodiester hydrolysis of the bis(2,4 − dinitrophenyl)phosphate (2,4 − BDNPP) substrate in the pH range 5.5–10.5. The kinetic studies further revealed that the homodinuclear [Ni(II)−Ni(II)] complexes (4) (kcat = 1.26 × 10−2 s−1) is more active by 39 times than the homodinuclear [Zn(II)−Zn(II)] complexes (3) (kcat = 3.20 × 10−4 s−1) and 27 times more active than the heterodinuclear [Zn(II)−Fe(III)] complex (2) (kcat = 4.62 × 10−4 s−1) in the phosphodiester hydrolysis activity. Significantly enough, the catalyst−substrate adduct species (2E, 2F and 3F) containing a metal bound bis(2,4‑dinitrophenyl)phosphate has been detected by mass spectrometry for the first time.

  • Conserved cysteine residues are necessary for nickel-induced allosteric regulation of the metalloregulatory protein YqjI (NfeR) in E. coli
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-26
    Matthew Blahut, Stephen Dzul, Suning Wang, Ashoka Kandegedara, Nicholas E. Grossoehme, Timothy Stemmler, F. Wayne Outten

    Transition metal homeostasis is necessary to sustain life. First row transition metals act as cofactors within the cell, performing vital functions ranging from DNA repair to respiration. However, intracellular metal concentrations exceeding physiological requirements may be toxic. In E. coli, the YqjH flavoprotein is thought to play a role in iron homeostasis. YqjH is transcriptionally regulated by the ferric uptake regulator and a newly discovered regulator encoded by yqjI. The apo-form of YqjI is a transcriptional repressor of both the yqjH and yqjI genes. YqjI repressor function is disrupted upon binding of nickel. The YqjI N-terminus is homologous to nickel-binding proteins, implicating this region as a nickel-binding domain. Based on function, yqjI and yqjH should be renamed Ni-responsive Fe-uptake regulator (nfeR) and Ni-responsive Fe-uptake flavoprotein (nfeF), respectively. X-ray Absorption Spectroscopy was employed to characterize the nickel binding site(s) within YqjI. Putative nickel binding ligands were targeted by site-directed mutagenesis and resulting variants were analyzed in vivo for repressor function. Isothermal titration calorimetry and competitive binding assays were used to further quantify nickel interactions with wild-type YqjI and its mutant derivatives. Results indicate plasticity in the nickel binding domain of YqjI. Residues C42 and C43 were found to be required for in vivo response of YqjI to nickel stress, though these residues are not required for in vitro nickel binding. We propose that YqjI may contain a vicinal disulfide bond between C42 and C43 that is important for nickel-responsive allosteric interactions between YqjI domains.

  • Structure and biological properties of five Pt(II) complexes as potential anticancer agents
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-25
    Jungang Deng, Jun Wang, MuhammadHamid Khan, Ping Yu, Feng Yang, Hong Liang

    We synthesized and validated five Schiff base Pt(II) complexes derived from 2-hydroxy-1-naphthaldehyde benzoyl hydrazone and its derivatives. The complexes were [Pt(L1)(DMSO)Cl] (C1), [Pt(L2)(DMSO)Cl] (C2), [Pt(L3)(DMSO)Cl] (C3), [Pt(L4)(DMSO)Cl] (C4), and [Pt(L5)(DMSO)Cl] (C5). Crystal structures showed that the Pt centers of all complexes were tetra-coordinated with other atoms. The structure-activity relationships and anticancer mechanisms of the complexes were explored. These five Pt(II) complexes were toxic at micromolar doses and exhibited cytotoxicity similar to or somewhat higher than that of cisplatin, with IC50 values ranging from 4.38 μM to 25.16 μM. The complexes exerted chemotherapeutic effects via inhibition of telomerase by targeting the c-myc promoter and down-regulating the expression of human telomerase reverse transcriptase, consequently triggering cell apoptosis. In addition, Pt(II) complexes also caused cell cycle arrest at S-phase, leading to the down-regulation of cdc25 A, cyclin A2, and CDK2 and up-regulation of p53, p27, and p21 proteins. Other complex-associated events were reactive oxygen species production, transformation of the mitochondrial membrane potential (Δψm), release of cytochrome c, regulation of Bcl-2 family protein expression, facilitated release of apoptotic active substances, and activation of caspases to induce apoptosis.

  • A combined computational and experimental study on selective flucloxacillin hydroxylation by cytochrome P450 BM3 variants
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-24
    Rosa A. Luirink, Stefan J. Dekker, Luigi Capoferri, Laura F.H. Janssen, Cynthia L. Kuiper, Mehmet E. Ari, Nico P.E. Vermeulen, J. Chris Vos, Jan N.M. Commandeur, Daan P. Geerke

    The 5′-hydroxymethyl metabolite of the penicillin based antibiotic flucloxacillin (FLX) is considered to be involved in bile duct damage occurring in a small number of patients. Because 5′-hydroxymethyl FLX is difficult to obtain by organic synthesis, biosynthesis using highly active and regioselective biocatalysts would be an alternative approach. By screening an in-house library of Cytochrome P450 (CYP) BM3 mutants, mutant M11 L437E was identified as a regioselective enzyme with relatively high activity in production of 5′-hydroxymethyl FLX as was confirmed by mass spectrometry and NMR. In contrast, incubation of M11 L437E and other mutants with oxacillin (OX, which differs from FLX by a lack of aromatic halogens) resulted in formation of two metabolites. In addition to 5′-hydroxymethyl OX we identified a product resulting from aromatic hydroxylation. In silico studies of both FLX and OX with three CYP BM3 mutants revealed substrate binding poses allowing for 5′-methyl hydroxylation, as well as binding poses with the aromatic moiety in the vicinity of the heme iron for which the corresponding product of aromatic hydroxylation was not observed for FLX. Supported by the (differences in) experimentally determined ratios of product formation for OX hydroxylation by M11 and its L437A variant and M11 L437E, Molecular Dynamics simulations suggest that the preference of mutant M11 L437E to bind FLX in its catalytically active pose over the other binding orientation contributes to its biocatalytic activity, highlighting the benefit of studying effects of active-site mutations on possible alternative enzyme-substrate binding poses in protein engineering.

  • Modeling the hydrogen sulfide binding to heme
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-21
    B.D. Ostojić, P. Schwerdtfeger, D.S. Đorđević

    The binding of hydrogen sulfide to a model heme compound is investigated by coupled-cluster singles-doubles augmented by a perturbative triple excitations, CCSD(T), and density functional theory, DFT. The minimum energy path for the H2S addition to an isolated heme center of the heme protein is evaluated by adopting as a model the heme compound FeP(Im) (P = porphyrin; Im = imidazole). The FeP(Im)-H2S aduct is bound by 13.7 kcal/mol at the CCSD(T) level of theory. Relaxed potential energy curves for the lowest lying spin states of the H2S to FeP(Im) binding using DFT reveal that the binding process is associated with a “double spin-crossover” reaction with the existence of long-distance van der Waals minima only 5–7 kcal/mol above the FeP(Im)-H2S ground state. The fact that the energy of the singlet ground state of FeP(Im)-H2S is so close in energy to the dissociation products FeP(Im) + H2S points towards the reversibility of the H2S adsorption/desorption process in biochemical reactions.

  • Linear gold(I) complex with tris-(2-carboxyethyl)phosphine (TCEP): Selective antitumor activity and inertness toward sulfur proteins
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-14
    S.Q. Gomes, L. Vitoriano, E.G.R. de Arruda, A.L.T.G. Ruiz, T. Candido, J.E. de Carvalho, W.R. Lustri, C. Abbehausen

    The search for modulating ligand substitution reaction in gold complexes is essential to find new active metallo compounds for medical applications. In this work, a new linear and hydrosoluble goldI complex with tris-(2-carboxyethylphosphine) (TCEP) was prepared and the crystal structure solved by single crystal X-ray diffraction. The AuI coordinates linearly to two phosphines by the phosphorus atoms. Spectroscopic evaluation by 1H, 13C, 31P NMR in solid and solution state, infrared, mass spectrometry is also reported. In vitro growth inhibition (GI50) in a panel of nine tumorigenic and one non-tumorigenic cell lines demonstrated the complex is highly selective to ovarium adenocarcinoma (OVCAR-3) with GI50 of 3.04 nmol mL−1. Biophysical evaluation with the sulfur-rich amino acids and proteins showed the compound does not interact with two types of zinc fingers, bovine serum albumin, N-acetyl-l-cysteine and also l-histidine, revealing to be inert to ligand substitution reactions with these molecules. The compound also showed no antibacterial activity. Besides, it inhibits 15% of the activity of a mixture of serine-β-lactamase and metallo-β-lactamase from Bacillus cereus in the enzymatic activity assay, similarly to EDTA. These results suggest AuTCEP is selective to MBL but the cell uptake is hindered, and the compound does not reach the periplasmic space of Gram-positive bacteria. The unique inert behavior of AuTCEP is interesting to the field and represent the modulation of the reactivity through coordination chemistry to decrease the toxicity associated with AuI complexes and its lack of specificity, generating very selective compounds.

  • Evaluation of 99mTc-sulfonamide and sulfocoumarin derivatives for imaging carbonic anhydrase IX expression
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-13
    Misaki Nakai, Jihne Pan, Kuo-Shyan Lin, John R. Thompson, Alessio Nocentini, Claudiu T. Supuran, Yasuo Nakabayashi, Tim Storr

    With the aim to prepare hypoxia tumor imaging agents, technetium(I) and rhenium(I) tricarbonyl complexes with dipyridylamine (L1 = N-{[1-(2,2-dioxido-1,2-benzoxathiin-6-yl)-1H-1,2,3-triazol-4-yl]methyl}-N-(2-pyridinylmethyl)-2-pyridinemethanamine; L3 = N-{[1-[N-(4-aminosulfonylphenyl)]-1H-1,2,3-triazol-4-yl]methyl}-N-(2-pyridinyl-methyl)-2-pyridinemethanamine), and iminodiacetate (H2L2 = N-{[1-(2,2-dioxido-1,2-benzoxathiin-6-yl)-1H-1,2,3-triazole-4-yl]methyl}-N-(carboxy-methyl)-glycine; H2L4 = N-{[1-[N-(4-aminosulfonylphenyl)]-1H-1,2,3-triazole-4-yl]methyl}-N-(carboxymethyl)-glycine) ligands appended to sulfonamide or sulfocoumarin carbonic anhydrase inhibitors were synthesized. The Re(I) complexes were characterized using 1H/13C NMR, MS, EA, and in one case the X-ray structure of [Et3NH][Re(CO)3(L2)] was obtained. As expected, the Re coordination geometry is distorted octahedral, with a tridentate iminodiacetate ligand in a fac arrangement dictated by the three strong-field CO ligands. Inhibition studies of human carbonic anhydrases (hCAs) showed that the Re sulfocoumarin derivatives were inactive against hCA-I, -II and -IV, but had moderate affinity for hCA-IX. The Re sulfonamides showed improved affinity against all tested hCAs, with [Re(CO)3(L4)]− being the most active and selective for the hCA-IX isoform. The corresponding 99mTc complexes were synthesized from fac-[99mTc(CO)3(H2O)3]+, purified by HPLC, and obtained with average 41–76% decay-corrected radiochemical yields and with >99% radiochemical purity. Uptake in HT-29 tumors at 1 h post-injection was highest for [99mTc(CO)3(L4)]− (0.14 ± 0.10%ID/g) in comparison to [99mTc(CO)3(L1)]+ (0.06 ± 0.01%ID/g), [99mTc(CO)3(L2)]− (0.03 ± 0.00%ID/g), and [99mTc(CO)3(L3)]+ (0.07 ± 0.03%ID/g). The uptake in tumors was further reduced at 4 h post-injection. For potential imaging application with single photon emission computed tomography, further optimization is needed to improve the affinity to hCA-IX and uptake in hCA-IX expressing tumors.

  • Refolding kinetics of cytochrome c studied with microsecond timescale continuous-flow UV–vis spectroscopy and rapid freeze-quench EPR
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-11
    Batoul Srour, Marc J.F. Strampraad, Wilfred R. Hagen, Peter-Leon Hagedoorn

    The study of the structure, function, folding and conformational transitions of cytochrome c is of great interest because this protein plays an important role in biological electron transport and apoptosis. The different native and non-native conformations have been studied extensively under equilibrium conditions at different pH values, however, kinetic studies are rare because they require technically challenging rapid mixing and spectroscopic monitoring techniques. Here we present the refolding kinetics of acid denatured cytochrome c using the pH jump technique from pH 2 to pH 4.7 in combination with a new ultrafast continuous flow mixing device that allows time resolved measurements to the microsecond time scale. Our results show that the initial refolding of denatured oxidized cytochrome c occurs very rapidly with a time constant τ = 10 μs, and is followed by discrete refolding steps with time constants of 56 and 208 μs. Electron paramagnetic resonance analysis of the different intermediates, obtained by microsecond freeze hyper quenching showed that the first two intermediates are predominantly high spin, and the third intermediate is the low spin species with complete His/Met coordination. The initial rapid phase is characterized by the formation of high spin species distinct from the completely unfolded state. We interpret this as the formation of a five coordinate species with His18 as the axial ligand or six coordinate with water and His18 as the axial ligands.

  • Role of the HSPA9/HSC20 chaperone pair in promoting directional human iron-sulfur cluster exchange involving monothiol glutaredoxin 5 ☆
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-11
    Joshua A. Olive, J.A. Cowan

    Iron‑sulfur clusters are essential cofactors found across all domains of life. Their assembly and transfer are accomplished by highly conserved protein complexes and partners. In eukaryotes a [2Fe-2S] cluster is first assembled in the mitochondria on the iron‑sulfur cluster scaffold protein ISCU in tandem with iron, sulfide, and electron donors. Current models suggest that a chaperone pair interacts with a cluster-bound ISCU to facilitate cluster transfer to a monothiol glutaredoxin. In humans this protein is glutaredoxin 5 (GLRX5) and the cluster can then be exchanged with a variety of target apo proteins. By use of circular dichroism spectroscopy, the kinetics of cluster exchange reactivity has been evaluated for human GLRX5 with a variety of cluster donor and acceptor partners, and the role of chaperones determined for several of these. In contrast to the prokaryotic model, where heat-shock type chaperone proteins HscA and HscB are required for successful and efficient transfer of a [2Fe-2S] cluster from the ISCU scaffold to a monothiol glutaredoxin. However, in the human system the chaperone homologs, HSPA9 and HSC20, are not necessary for human ISCU to promote cluster transfer to GLRX5, and appear to promote the reverse transfer. Cluster exchange with the human iron‑sulfur cluster carrier protein NFU1 and ferredoxins (FDX's), and the role of chaperones, has also been evaluated, demonstrating in certain cases control over the directionality of cluster transfer. In contrast to other prokaryotic and eukaryotic organisms, NFU1 is identified as a more likely physiological donor of [2Fe-2S] cluster to human GLRX5 than ISCU.

  • Liposomal formulations of magnesium sulfanyl tribenzoporphyrazines for the photodynamic therapy of cancer
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-09
    Jaroslaw Piskorz, Dariusz T. Mlynarczyk, Wojciech Szczolko, Krystyna Konopka, Nejat Düzgüneş, Jadwiga Mielcarek

    Photodynamic therapy of cancer comprises the activation of photosensitizer molecules delivered to cancer cells, to generate reactive oxygen species that mediate cytotoxicity. In this study, previously synthesized dendritic magnesium tribenzoporphyrazines were incorporated into four types of liposomes containing either 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) or 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE) as the zwitterionic lipids. The addition of either l-α-phosphatidyl-dl-glycerol (PG) or 1,2-dioleoyl-3-trimethylammoniumpropane (DOTAP) imparted a negative or positive charge, respectively. Novel formulations were tested in oral squamous cell carcinoma cell lines (CAL 27, HSC-3) as well as cervical adenocarcinoma cells (HeLa). Positively charged DOTAP:POPC liposomes were the most effective carriers for all tested tribenzoporphyrazines. Calculated IC50 values for DOTAP:POPC liposomes indicated that the incorporation of tribenzoporphyrazines into these liposomes can improve photocytotoxicity up to 50-fold compared to the free forms of macrocycles. Oral cancer cells (CAL 27 and HSC-3) were more sensitive to liposomal photodynamic treatment than HeLa cells.

  • Anti-cancer activity of di- and tri-organotin(IV) compounds with d-(+)-Galacturonic acid on human tumor cells
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-09
    Maristella Ippolito, Maria Assunta Girasolo, Filippo Saiano, Alessandro Attanzio, Archimede Rotondo, Simona Rubino, Luigi Mondello, Massimo L. Capobianco, Piera Sabatino, Luisa Tesoriere, Girolamo Casella

    We have compared the anti-proliferative activity in vitro, of R2SnGala (1–3) [R = Me, n-Bu, pH] and novel R3SnGala (4, 5) [R = Me, n-Bu] with D-(+)-Galacturonic acid [HGala; Galaq-, q = (2) and (1) for R2SnGala and R3SnGala, respectively] compounds, towards human tumor cell lines of intestinal carcinoma (HCT-116) and breast adenocarcinoma (MCF-7). The new synthesized 4 and 5 compounds were characterized, in solution, by 1H,13C and 119Sn NMR, that showed that HGala acts as monoanionic moiety and evidenced the dynamic behavior of the compounds, due to inter-conversions involving the anomeric carbon atom of the ligand. Cell viability, apoptosis induction and cell cycle distribution were analyzed by MTT colorimetric assay and flow cytometry, respectively. The cytotoxicity of the compounds, in the micro-submicromolar range, changed in the order of the organotin(IV) moieties, according to 5 > 3 > 2, while 1 and 4, containing MenSn(IV) (n = 2,3) moieties, were ineffective. Compound 5 showed peculiar cytotoxic effects. It did not cause time dependent inhibition of cell growth nor accumulated into the cells. Cell death induced by the active 2, 3, and 5, was shown to be apoptotic by measuring the exposure of phosphatidylserine to the outer membrane and the loss of mitochondrial potential. All the cytotoxic compounds induced an accumulation of cells in the subG0/G1phase, while only 2 and 3 perturbed the cell cycle confining viable cells in G0/G1phase. Finally, none of the compounds investigated affected the viability of normal intestinal or liver cells, indicating selectivity towards tumor cells.

  • Alpha lipoic acid attenuates cadmium-induced nephrotoxicity via the mitochondrial apoptotic pathways in rat
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-07
    Shihao Chen, Gang Liu, Mengfei Long, Hui Zou, Hengmi Cui

    Alpha lipoic acid (α-LA), a potent antioxidant, is protective against acute nephrotoxicity. In the present study, the attenuation of cadmium (Cd)-induced kidney injury by α-LA on was investigated in a rat model. Exposure to 50 mg/L Cd for 12 weeks increased kidney index and Cd content, malondialdehyde (MDA) levels, and histological damage to the renal cortex, and decreased the activities of glutathione peroxidase (GSH-Px), superoxide dismutase (SOD), catalase (CAT), and glutathione (GSH). Treatment with 50 mg/L Cd also damaged renal cell mitochondria and nuclei, and activated the mitochondrial apoptosis pathway, indicated by increased gene and protein expression/activation of caspase-9, caspase-3, poly ADP-ribose polymerase (PARP) and Bcl-2 adenovirus E1a nineteen kilodalton interacting protein 3 (BNIP3), and translocation of cytochrome c (cyt c), apoptosis-inducing factor (AIF), and endonuclease G (Endo G). However, simultaneous supplementation with α-LA (50 mg/kg·bw) protected kidney cells from Cd-induced cytotoxicity by reducing MDA levels and Cd content, restoring endogenous enzyme activities, renewing mitochondrial function, and preventing activation of the mitochondria apoptosis pathway.

  • Biophysical characterization of Aptenodytes forsteri cytochrome P450 aromatase
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-07
    Francisco Zarate-Perez, Jesús B. Velázquez-Fernández, Gareth K. Jennings, Lisa S. Shock, Charles E. Lyons, John C. Hackett

    Cytochrome P450 19 (CYP19, aromatase) catalyzes the conversion of androgens to estrogens in a sequence of three reactions that each depend on NADPH and O2. Aromatase is a phylogenetically-ancient enzyme and its breadth of expression in other species has highlighted distinct physiological functions. In songbirds, estrogen production is required for programming the neural circuits controlling song and in the determination of sex in fish and reptiles. This work describes the expression, purification, and biophysical characterization of Aptenodytes forsteri (Emperor penguin) aromatase. Using human cytochrome P450 reductase as a redox partner, afCYP19 displayed similar substrate turnover and LC/MS/MS confirmed that afCYP19 catalyzes the transformations through the intermediates 19-hydroxy- and 19-oxo-androstenedione. Androstenedione and anastrozole had the highest affinity for the enzyme and were followed closely by 19-hydroxyandrostenedione and testosterone. The affinity of 19-oxo-androstenedione for afCYP19 was ten-fold lower. The time-dependent changes in the Soret bands observed in stopped-flow mixing experiments of the steroidal ligands and the inhibitor anastrozole with afCYP19 were best described by a two-step binding mechanism. In summary, these studies describe the first biophysical characterization of an avian aromatase that displays strikingly similar enzyme kinetics and ligand binding properties to the human enzyme and could serve as a convenient model system for studies of the enigmatic transformation of androgens to estrogens.

  • Cross-talk of cannabinoid and endocannabinoid metabolism is mediated via human cardiac CYP2J2
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-07
    William R. Arnold, Austin T. Weigle, Aditi Das

    Phytocannabinoids have well-known cardiovascular implications. For instance, Δ9-tetrahydrocannabinol (Δ9-THC), the principal component of cannabis, induces tachycardia in humans. In order to understand the impact of phytocannabinoids on human cardiovascular health, there is a need to study the metabolism of phytocannabinoids by cardiac cytochromes p450 (CYPs). CYP2J2, the primary CYP of cardiomyocytes, is responsible for the metabolism of the endocannabinoid, anandamide (AEA), into cardioprotective epoxides (EET-EAs). Herein, we have investigated the kinetics of the direct metabolism of six phytocannabinoids (Δ9-THC, Δ8-tetrahydrocannabinol, cannabinol, cannabidiol, cannabigerol, and cannabichromene) by CYP2J2. CYP2J2 mainly produces 1′/1″-OH metabolites of these phytocannabinoids. These phytocannabinoids are metabolized with greater catalytic efficiency compared to the metabolism of AEA by CYP2J2. We have also determined that the phytocannabinoids are potent inhibitors of CYP2J2-mediated AEA metabolism, with Δ9-THC being the strongest inhibitor. Most of the inhibition of CYP2J2 by the phytocannabinoids follow a noncompetitive inhibition model, and therefore dramatically reduce the formation of EET-EAs by CYP2J2. Taken together, these data demonstrate that phytocannabinoids are directly metabolized by CYP2J2 and inhibit human cardiac CYP2J2, leading to a reduction in the formation of cardioprotective EET-EAs.

  • Influence of copper(II) ions on the noncovalent interactions between cytidine-5′-diphosphate or cytidine-5′-triphosphate and biogenic amines putrescine or spermidine
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-06
    R. Bregier-Jarzębowska, L. Łomozik, A. Gąsowska

    Potentiometric and NMR spectroscopic studies of the nucleotide (NucP)/polyamine (PA) system (where NucP = CDP, CTP, PA = putrescine or spermidine) revealed the formation of molecular complexes (NucP)(Hx+y)(PA) (where Hx+y = number of protons; x - from NucP and y - from PA). Their thermodynamic parameters were determined and the modes of their interactions were proposed. The main reaction centers were found to be the protonated amine groups of polyamine (positive centers) and phosphate groups of nucleotide (negative centers). The pH ranges in which the complex occurs correspond to those of amine protonation and -PO3x- group deprotonation, which unambiguously confirms the dipole-dipole type of interaction. In the pH range of total deprotonation of single bond NHx+ groups from the polyamine, the molecular complexes disappear. The equilibrium and spectroscopic studies of the ternary systems Cu(II)/NucP/PA evidenced the formation of Cu(NucP)Hx+y(PA) type coordination compounds and Cu(NucP)⋯(PA)(Hx) type molecular complexes with polyamine in the outer coordination sphere. The main sites of metal ion bonding in the latter species are the phosphate groups of the nucleotide, while in the coordination compounds – besides the phosphate groups – also the donor nitrogen atoms from the polyamines. In this paper we have also quantitatively calculated the effect of metal ions on the formation of the molecular complexes.

  • Evolution of phosphotriesterase activities of the metallo-β-lactamase family: A theoretical study
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-06
    Hao Zhang, Ling Yang, Long-Fei Yan, Rong-Zhen Liao, Wei-Quan Tian

    Metallo-β-lactamase (MβL) is a eubacterial zinc metallo-hydrolase superfamily. Despite their well-known lactamase activities, MβL family members also have the ability to catalyze phosphotriester hydrolysis with different phosphotriesterase activities. In the present study, based on crystal structure comparisons of the related MβL members, a series of models was constructed and calculated using the density functional theory (DFT) method to explore the relationship between active-site changes and phosphotriesterase activities. These calculations show that the energetic barriers for phosphotriesterase activity are considerably reduced due to active-site differences, which describes an evolutionary trend for the development of phosphotriesterase activity in the MβL superfamily. The key event is the appearance of a specialized and negatively charged residue bridging both zinc ions, which plays the two important roles of maintaining charge balance and stabilizing the binuclear active-site structure. This pathway is also consistent with the evolutionary relationships determined by phylogenetic tree analysis using complete residue sequences. Our studies provide the first methodology to explore the development of a new enzyme activity within a superfamily, and to shed new light on understanding the catalytic mechanism from an evolutionary perspective.

  • EPR evidence for a fast-relaxing iron center in Na+-translocating NADH:quinone-oxidoreductase
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-06
    Leonid V. Kulik, Yulia V. Bertsova, Alexander V. Bogachev

    A paramagnetic Cys4[Fe] center was detected by pulse EPR in Na+-translocating NADH:quinone-oxidoreductase (Na+-NQR) by influence of this center on transverse and longitudinal spin relaxation of Na+-NQR flavin radicals. The oxidation state of the Cys4[Fe] center was Fe3+ in the oxidized and Fe2+ in the reduced Na+-NQR, as deduced from the temperature dependence of spin relaxation rates of different flavin radicals. A high-spin state of iron in the Cys4[Fe] center was assigned to both forms of Na+-NQR.

  • New (arene)ruthenium(II) complexes of 4‑aryl‑4H‑naphthopyrans with anticancer and anti-vascular activities
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-04-05
    Florian Schmitt, Jana Kasparkova, Viktor Brabec, Gerrit Begemann, Rainer Schobert, Bernhard Biersack

    A series of four 2‑amino‑3‑cyano‑4‑(3/4‑pyridyl)‑4H‑benzo[h]chromenes 2a–d and their dichlorido(p‑cymene)ruthenium(II) complexes 3a–d were tested for antiproliferative, vascular-disruptive, anti-angiogenic and DNA-binding activity. The coordination of the 4‑pyridyl‑4H‑naphthopyrans 2 to ruthenium led to complexes with pleiotropic effects. Unlike the free ligands 2a–d, their ruthenium complexes 3a–d showed a significant affinity for DNA as demonstrated by electrophoretic mobility shift assays (EMSA) and ethidium bromide assays. Binding of 3a–d to calf thymus DNA proceeded about 10-times faster compared with cisplatin. Treatment of HT-29 colon carcinoma, 518A2 melanoma and MCF-7Topo breast cancer cells with 3a and 3b caused an accumulation of cells in the G2/M phase and an increase of the fraction of mitotic cells in the case of HT-29, due to alterations of the microtubule cytoskeleton as shown by immunofluorescence staining. Complexes 3b–c showed a dual effect on the vascular system. They suppressed angiogenesis in zebrafish embryos and they destroyed the vasculature of the chorioallantoic membrane (CAM) in fertilized chicken eggs. They also inhibited the vasculogenic mimicry, typical of U-87 glioblastoma cells in tube formation assays.

  • Titanocene binding to oligonucleotides
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-28
    Rahel P. Eberle, Stefan Schürch
  • Side chain removal from corticosteroids by unspecific peroxygenase
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-26
    René Ullrich, Marzena Poraj-Kobielska, Steffi Scholze, Claire Halbout, Martin Sandvoss, Marek J. Pecyna, Katrin Scheibner, Martin Hofrichter
  • A docked state conformational dynamics model to explain the ionic strength dependence of FMN-heme electron transfer in nitric oxide synthase
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-26
    Andrei V. Astashkin, Jinghui Li, Huayu Zheng, Yubin Miao, Changjian Feng
  • Photo-antimicrobial efficacy of zinc complexes of porphyrin and phthalocyanine activated by inexpensive consumer LED lamp
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-24
    Lijo George, Arto Hiltunen, Ville Santala, Alexander Efimov
  • Synthesis, characterization and DNA interactions of [Pt3(TPymT)Cl3], the trinuclear platinum(II) complex of the TPymT ligand
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-17
    Tiziano Marzo, Damiano Cirri, Lorenzo Ciofi, Chiara Gabbiani, Alessandro Feis, Nancy Di Pasquale, Matteo Stefanini, Tarita Biver, Luigi Messori
  • Three new platinum complexes containing fluoroquinolones and DMSO: Cytotoxicity and evaluation against drug-resistant tuberculosis
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-16
    Leticia P. de Oliveira, Zumira A. Carneiro, Camila M. Ribeiro, Maurício F. Lima, Drielly A. Paixão, Marcos Pivatto, Marcus V.N. de Souza, Letícia R. Teixeira, Carla D. Lopes, Sérgio de Albuquerque, Fernando R. Pavan, Wendell Guerra
  • 更新日期:2018-03-16
  • A study of the properties, reactivity and antitumor activity of novel N-methylated-3-thiazolyl or 3-thienyl carbazoles and their Pd(II) and Pt(II) complexes
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-15
    M. Reig, R. Bosque, M. Font-Bardía, C. Calvis, R. Messeguer, L. Baldomà, J. Badía, D. Velasco, C. López
  • 更新日期:2018-03-15
  • Insights from kinetic studies of photo-generated compound II models: Reactivity toward aryl sulfides
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-09
    Ngo Fung Lee, Dharmesh Patel, Haiyan Liu, Rui Zhang
  • Biological evaluation of water soluble Arene Ru(II) enantiomers with amino-oxime ligands
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-06
    Isabel de la Cueva-Alique, Sara Sierra, Laura Muñoz-Moreno, Adrián Pérez-Redondo, Ana M. Bajo, Isabel Marzo, Lourdes Gude, Tomás Cuenca, Eva Royo
  • Gradient coatings of strontium hydroxyapatite/zinc β-tricalcium phosphate as a tool to modulate osteoblast/osteoclast response
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-06
    Elisa Boanini, Paola Torricelli, Felix Sima, Emanuel Axente, Milena Fini, Ion N. Mihailescu, Adriana Bigi
  • 更新日期:2018-03-07
  • Membrane-attached mammalian cytochromes P450: An overview of the membrane's effects on structure, drug binding, and interactions with redox partners
    J. Inorg. Biochem. (IF 3.063) Pub Date : 2018-03-05
    Martin Šrejber, Veronika Navrátilová, Markéta Paloncýová, Václav Bazgier, Karel Berka, Pavel Anzenbacher, Michal Otyepka
Some contents have been Reproduced with permission of the American Chemical Society.
Some contents have been Reproduced by permission of The Royal Society of Chemistry.
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