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The focus of this book is on the assembly and role of metalloproteins which contain either an iron atom in a mononuclear or binuclear metal-active site, or for those metalloproteins where the assembly and final activity of the enzyme is dependent on an FeS cluster containing protein. It investigates the crosstalk in the assembly of metal-active sites and the role of different metal ions in polynuclear metallo clusters. Additionally, the book also explains the availability of metal-ions is tightly regulated and the metal homeostasis and trafficking in a cellular context
List of contents
Volume I
1.ISC-based Fe-S cluster assembly and insertion in prokaryotes
2.SUF-based Fe-S cluster assembly in prokaryotes
3.Mitochondrial Fe-S cluster assembly in eukaryotes
4.Cytosolic Fe-S cluster assembly in eukaryotes
5.Aldehyde oxidase
6.Sulfur acquisition in methanogens
7.Moco Biosynthesis in bacteria
8.Moco Biosynthesis in eukaryotes
9.Biosynthesis of Fe-S clusters by NifS/U
10.Alternative substrates of nitrogenases
Volume II
1.Bifurcating hydrogenases
2.Biosynthesis of [FeFe]-hydrogenase
3.Biosynthesis of [NiFe]-hydrogenase
4.Biosynthesis of [Fe]-hydrogenase
5.Hydrogenase reaction mechanism
6.Introduction into X-ray Chrystallography
7.Vibrational Spectroscopy
8.Theoretical studies
9.Model compounds and inorganic chemistry
10.Formate dehydrogenases
About the author
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.
