Iron-Sulfur Clusters: Biogenesis and Biochemistry

Author:   Silke Leimkühler (Ruhr-University of Bochum, Germany; Duke University Medical Center, NC, USA) ,  Günter Schwarz (University of Cologne, Germany) ,  Oliver Lenz (Technische Universität Berlin, Germany) ,  Oliver Einsle (Max-Planck-Institute for Biochemistry, Germany)
Publisher:   Wiley-VCH Verlag GmbH
ISBN:  

9783527352555


Pages:   800
Publication Date:   22 October 2025
Format:   Hardback
Availability:   Out of stock   Availability explained
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Iron-Sulfur Clusters: Biogenesis and Biochemistry


Overview

An authoritative and up-to-date collection of resources covering the ubiquitous iron-sulfur cluster-containing proteins In Iron-Sulfur Clusters: Biogenesis and Biochemistry, a team of distinguished researchers delivers an incisive and practical discussion of the assembly and role of metalloproteins containing an iron atom in a mononuclear or binuclear metal-active site, or where the assembly and final activity of the enzyme depends on an Fe-S cluster containing protein. The book examines the crosstalk in the assembly of metal-active sites and the roles played by various metal ions in polynuclear metalloclusters. It also describes metal homeostasis and trafficking in a cellular context and explains why the availability of metal ions is tightly regulated. Of particular interest to chemists working with iron-sulfur (Fe-S) clusters in biology, biochemistry, pharmaceuticals, and drug synthesis, the book also contains: A thorough introduction to the biosynthesis of hydrogenase cofactors and hydrogenase reaction mechanisms Comprehensive explorations of the reaction mechanisms of molybdoenzymes, including sulfite oxidase, aldehyde oxidase, and formate dehydrogenase Practical discussions of the biosynthesis of Fe-S clusters in prokaryotes and eukaryotes Complete examinations of the insertion of Fe-S clusters and the biosynthesis of Moco and FeMoco An overview of the chemical, crystallographic, spectroscopic and theoretical methods commonly used to characterize Fe-S clusters. Perfect for biochemists and protein, pharmaceutical, bioinorganic, and organic chemists, Iron-Sulfur Clusters will also be useful for food and environmental chemists, as well as professionals working in the pharmaceutical industry.

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Author:   Silke Leimkühler (Ruhr-University of Bochum, Germany; Duke University Medical Center, NC, USA) ,  Günter Schwarz (University of Cologne, Germany) ,  Oliver Lenz (Technische Universität Berlin, Germany) ,  Oliver Einsle (Max-Planck-Institute for Biochemistry, Germany)
Publisher:   Wiley-VCH Verlag GmbH
Imprint:   Blackwell Verlag GmbH
Dimensions:   Width: 17.00cm , Height: 1.50cm , Length: 24.40cm
Weight:   0.680kg
ISBN:  

9783527352555


ISBN 10:   3527352554
Pages:   800
Publication Date:   22 October 2025
Audience:   Professional and scholarly ,  Professional & Vocational
Format:   Hardback
Publisher's Status:   Active
Availability:   Out of stock   Availability explained
The supplier is temporarily out of stock of this item. It will be ordered for you on backorder and shipped when it becomes available.

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Author Information

Silke Leimkühler, PhD, is a Full Professor in Molecular Enzymology at the University of Potsdam in Germany. Her research is focused on molybdenum cofactor biosynthesis, molybdoenzyme enzymology, cellular sulfur transfer mechanisms for sulfur-containing biomolecule synthesis, and related subjects. Günter Schwarz is Professor for Biochemistry at the University of Cologne. His research is focused on molecular biology, protein biochemistry, enzymology, structural biology, cell biology, and more. Oliver Lenz is the Head of the Research Group Biochemistry of Gas-Converting Biocatalysts at the Technische Universität Berlin. His research is focused on the role of molecular hydrogen in the metabolism of microorganisms. Oliver Einsle is a Full Professor of Biochemistry in Freiburg, Germany and the Director of the Institute of Biochemistry in the Faculty of Chemistry and Pharmacy. His research is focused on the structural and functional characterization of metalloproteins, like nitrogenase and nitrous oxide reductase.

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