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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
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Produktbeschreibung
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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Autorenporträt
Silke Leimkühler received her Ph.D in microbiology at the Ruhr-University of Bochum, Germany in 1998. After a post-doctoral position in the Department of Biochemistry at the Duke University Medical Center (Durham, NC, USA) from 1999-2001, she returned to Germany with an Emmy-Noether grant from the DFG to establish her own research group at the Technical-University of Braunschweig, where she stayed until 2004. In 2005 she accepted a Junior-Professor position at the University of Potsdam, Germany. Since 2009 she has a full professor position in Molecular Enzymology at the University of Potsdam, Germany. Her major research interests focus on molybdenum cofactor biosynthesis, molybdoenzyme enzymology, cellular sulfur transfer mechanisms for sulfur-containing biomolecule synthesis and the role of Fe-S cluster assembly on molybdoenzyme maturation.

Guenter Schwarz is the Professor for Biochemistry at the University of Cologne. his research is based on a variety of methods including molecular biology, protein biochemistry, enzymology, structural biology (protein crystallography), cell biology, bioinorganic chemistry and biotechnology. Interdisciplinarity is a key to investigate complex biological problems and therefore his lab has established collaborations with groups working in diverse field such as Human Genetics, Neurobiology, Crystallography, Spectroscopy and Medicine.

Oliver Lenz is the Head of the Research Group ?Biochemistry of Gas-Converting Biocatalysts? at the Technische Universität Berlin. His main research focus is on the pivotal role of molecular hydrogen in in the metabolism of many microorganisms, including bacteria, archaea and lower eukaryotes. He completed his PhD in 1998 Doctor in Biology (Microbiology under the supervision of Prof. Dr. Bärbel Friedrich, Humboldt-Universität Berlin, Germany. Oliver was a group leader at the Institute of Biology/Microbiology, Humboldt-Universität zu Berlin.

Oliver Einsle studied Biology in Konstanz, Germany, and then moved to the Max- Planck-Institute for Biochemistry in Martinsried, Germany, to work with Robert Huber and Peter Kroneck on cytochrome c nitrite reductase. In 2001 he joined the laboratory of Douglas Rees at Caltech, USA, to study nitrogenase, and in 2003 he was appointed junior professor for protein crystallography in Göttingen, Germany. Since 2008 he is full professor of Biochemistry in Freiburg, Germany, and director of the Institute of Biochemistry in the faculty of Chemistry and Pharmacy. His group has made seminal contributions to the structural and functional characterization of various metalloproteins, including nitrogenase and nitrous oxide reductase, but also multiheme cytochromes c. A second line of research is centered on the study of integral membrane proteins, in particular bacterial transporters and channels.