Biological transition metal-sulfur sites are known for almost all so-called essential transition metal ions. Metalloenzymes based on such metal-sulfur sites catalyze some red-hot chemical reactions and a better understanding of the related processes might therefore solve existential problems of mankind in future. Enzymes with metal-sulfur sites promising such an impact are for example nitrogenases with P-cluster and a [Mo-7Fe-9S-C]-homocitrate catalytic site or carbon monoxide dehydrogenases and hydrogenases with NiFeS sites, just to name a few examples. Therefore, the 20th volume of the ‘Metal Ions in Life Sciences’ series edited by ‘the Sigels’ (Astrid Sigel, Eva Freisinger, Roland K.O. Sigel) is dedicated to sulfur and metal-sulfur sites and covers many aspects and a tremendous amount of information one could hardly extract and compile oneself in 12 chapters. Thus, this 20th volume certainly fills a gap in the metal ions in life science field and answers several questions a lecturer could be confronted with, in bioinorganic courses. Chapter 1 by the volume editors Martha E. Sosa Torres and Peter M. H. Kroneck themselves resembles more or less an appetizer for this volume. In this introductory chapter, the sulfur-based focus of the volume is defined which clearly lies in the blue copper proteins, the CuA copper-sulfide centre of cytochrome c oxidase (COX) or nitrous oxide reductase N2OR, the tetranuclear copper-sulfide center CuZ of N2OR, the cytochrome P450 enzyme superfamily, iron sulfur clusters such as the siroheme-[4Fe-4S] centre, molybdenum and tungsten enzyme sites bearing the pterin dithiolene cofactor as well as the enzyme sites already mentioned above. Moreover, evolutionary connections and possible future directions are highlighted here. Chapter 2 was also authored by Martha E. Sosa Torres and Peter M. H. Kroneck in cooperation with Alfonso R. Morales and Alejandro S. Peralta. It starts with a small essay about the various faces sulfur can exhibit in mineralogy and bio-mineralization as well as in organic and inorganic chemistry. This leads to microbial sulfur metabolism and aerobic oxidation as well as anaerobic reduction of sulfur for energy conservation purposes. This is exemplary discussed by means of a sulfur oxygenase and a polysulfide reductase. Microbial sulfate activation via adenosine 5′-phosphosulfate (APS) and sulfite reductases fit in this context, too. Then, cofactors and coenzymes with sulfur are reviewed such as biotin and thiamine. The chapter is then completed with the S-adenosyl-L-methionine (SAM) and its role in the radical SAM pathway. Chapter 3 by Trinidad Arcos-López, Nils Schuth and Liliana Quintanar focuses on the type 1 blue copper (T1 Cu) sites in biology, especially the electron transfer (ET) properties of these sites and their unique spectroscopic features. As summarized nicely by the authors, these are controlled by entatic state geometry and a highly covalent Cu–S bond * Nicolai Burzlaff nicolai.burzlaff@fau.de

中文翻译：

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Martha E. Sosa Torres 和 Peter MH Kroneck（客座编辑）、Astrid Sigel、Eva Freisinger 和 Roland KO Sigel（系列编辑）：过渡金属和硫：生命的牢固关系，卷。生命科学中的20种金属离子

生物过渡金属硫位点以几乎所有所谓的基本过渡金属离子而闻名。基于这种金属硫位点的金属酶催化了一些炽热的化学反应，因此更好地了解相关过程可能会在未来解决人类的生存问题。具有金属硫位点的酶有望产生这种影响，例如具有 P 簇和 [Mo-7Fe-9S-C]-高柠檬酸催化位点的固氮酶或具有 NiFeS 位点的一氧化碳脱氢酶和氢化酶，仅举几个例子。因此，由'the Sigels'（Astrid Sigel、Eva Freisinger、Roland KO）主编的《生命科学中的金属离子》系列第20卷 Sigel) 致力于硫和金属硫位点，涵盖了很多方面和大量的信息，在 12 章中很难提取和编译。因此，这第 20 卷无疑填补了生命科学领域金属离子的空白，并回答了讲师在生物无机课程中可能面临的几个问题。卷编辑 Martha E. Sosa Torres 和 Peter MH Kroneck 的第 1 章本身或多或少类似于本卷的开胃菜。在这个介绍性章节中，该卷的硫基重点被定义为蓝铜蛋白、细胞色素 c 氧化酶 (COX) 或一氧化二氮还原酶 N2OR 的 CuA 硫化铜中心、四核硫化铜中心 CuZ N2OR，细胞色素 P450 酶超家族，铁硫簇，如 siroheme-[4Fe-4S] 中心、钼和钨酶位点，带有蝶呤二硫烯辅因子以及上面已经提到的酶位点。此外，这里强调了进化联系和可能的未来方向。第 2 章还由 Martha E. Sosa Torres 和 Peter MH Kroneck 与 Alfonso R. Morales 和 Alejandro S. Peralta 合作撰写。它以一篇关于硫在矿物学和生物矿化以及有机和无机化学中可能表现出的各种面的小文章开始。这导致微生物硫代谢和有氧氧化以及出于节能目的的硫的厌氧还原。这通过硫加氧酶和多硫化物还原酶进行示例性讨论。通过腺苷 5'-磷酸硫酸盐 (APS) 和亚硫酸盐还原酶激活微生物硫酸盐也适用于这种情况。然后，回顾了含硫的辅因子和辅酶，如生物素和硫胺素。本章最后介绍了 S-腺苷-L-甲硫氨酸 (SAM) 及其在自由基 SAM 通路中的作用。Trinidad Arcos-López、Nils Schuth 和 Liliana Quintanar 撰写的第 3 章重点介绍了生物学中的 1 型蓝铜 (T1 Cu) 位点，尤其是这些位点的电子转移 (ET) 特性及其独特的光谱特征。正如作者很好地总结的那样，这些是由立体状态几何和高度共价的 Cu-S 键控制的 * Nicolai Burzlaff nicolai.burzlaff@fau.de 本章最后介绍了 S-腺苷-L-甲硫氨酸 (SAM) 及其在自由基 SAM 通路中的作用。Trinidad Arcos-López、Nils Schuth 和 Liliana Quintanar 撰写的第 3 章重点介绍了生物学中的 1 型蓝铜 (T1 Cu) 位点，尤其是这些位点的电子转移 (ET) 特性及其独特的光谱特征。正如作者很好地总结的那样，这些是由立体状态几何和高度共价的 Cu-S 键控制的 * Nicolai Burzlaff nicolai.burzlaff@fau.de 本章最后介绍了 S-腺苷-L-甲硫氨酸 (SAM) 及其在自由基 SAM 通路中的作用。Trinidad Arcos-López、Nils Schuth 和 Liliana Quintanar 撰写的第 3 章重点介绍了生物学中的 1 型蓝铜 (T1 Cu) 位点，尤其是这些位点的电子转移 (ET) 特性及其独特的光谱特征。正如作者很好地总结的那样，这些是由立体状态几何和高度共价的 Cu-S 键控制的 * Nicolai Burzlaff nicolai.burzlaff@fau.de