Short CommunicationProtein dynamics of [Cu-Zn] superoxide dismutase (SOD1): How protein motions at the global and local levels impact the reactivity of SOD1
Graphical abstract
Secondary sphere interactions in a biomimetic model compound coupled with normal mode analysis of superoxide dismutase demonstrates how collective domain motion influences catalytic activity through conformational change and substrate guidance at the active site.
Section snippets
Credit authorship contribution statement
Eamonn F. Healy: Conceptualization, Methodology, Visualization, Formal analysis, Data curation, Writing - original draft, review & editing. Rafael Flores: Investigation. Vincent M. Lynch: Investigation. Santiago Toledo: Conceptualization, Methodology, Supervision, Validation, Writing - original draft, review & editing, Funding acquisition.
Declaration of competing interest
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Acknowledgement
The authors wish to acknowledge the support of the National Institute of General Medical Sciences of the National Institutes of Health (SC2GM130438), the National Science Foundation (#1832282), as well as Welch Foundation (Grant# BH-0018) for its continuing support of the Chemistry Department at St. Edward's University. This work used the Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1548562.
References (17)
- et al.
Superoxide dismutases—a review of the metal-associated mechanistic variations
Biochim. Biophys. Acta, Proteins Proteomics
(2010) - et al.
Coupled motions in enzyme catalysis
Curr. Opin. Chem. Biol.
(2010) - et al.
Conformational variability of the cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function
J. Mol. Biol.
(2000) - et al.
A model for gain of function in superoxide dismutase Biochem
Biochem. Biophys. Rep.
(2020) - et al.
Crystallographic structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal
J. Mol. Biol.
(1999) - et al.
Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu–Zn, Zn–Zn and as-isolated wild-type enzymes
J. Mol. Biol.
(2006) - et al.
Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
Annu. Rev. Biochem.
(2005) - et al.
A structure-based mechanism for copper− zinc superoxide dismutase
Biochemistry
(1999)