Nature’s way of handling a greenhouse gas: the copper-sulfur cluster of purple nitrous oxide reductase
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Anja Wüst
Anja Wüst (born 1983) completed an industrial training as chemical laboratory worker at BASF Ludwigshafen. Since July 2011 she works as a doctoral student in the group of Oliver Einsle, after she finished her diploma in Chemistry at the Albert-Ludwigs-University in Freiburg. Her field of interest are the mechanistic details of nitrous oxide reductase and the spectroscopic properties of its copper clusters.
Lisa Schneider (born 1986) studied Chemistry in Freiburg and obtained her diploma in 2011. Currently she works as a doctoral student with Oliver Einsle, and the focus of her thesis work is the characterization of the protein systems required for maturation and assembly of nitrous oxide reductase.
Anja Pomowski (born 1981) studied Biology in Göttingen and did her doctoral work with Oliver Einsle in Freiburg, where she worked on the structural characterization of nitrous oxide reduc-tase from Pseudomonas stutzeri. She currently works as a postdoctoral fellow with Jim Hunting-ton in Cambridge, UK.
Walter G. Zumft has been full professor of microbiology at the Karlsruhe Institute of Technology from 1982 until his retirement in 2007. He studied biology and physiological chemistry at the universities of Berlin (FU), Munich (LMU) and Erlangen and was a postdoc from 1971 to 1974 at Purdue University. He held visiting professorships at the Arrhenius Laboratory in Stockholm, the University of Georgia in Athens, and the University of Seville. His research interests center around the microbial biochemistry and molecular biology of inorganic nitrogen metabolism, where his main contributions concern nitrogenase, nitric oxide reductase, and nitrous oxide reductase.
Peter M.H. Kroneck studied Chemistry in Basel from 1962–1967 and obtained his doctorate in 1971 at Konstanz university with Peter Hemmerich. From 1971–1973 he worked as a postdoc with Jack T. Spence at Utah State University in Logan. He habilitated in Konstanz in 1980 and was appointed professor of Biochemistry in 1987. He retired in 2009 and has held various inter-national teaching appointments since. His main research interests are with the characterization of novel metalloenzymes using spectroscopic techniques
Oliver Einsle (born 1970) studied Biology in Konstanz with Peter Kroneck, then moved to the MPI for Biochemistry in Martinsried to work with Robert Huber and Peter Kroneck on nitrite re-ductases. In 2001 he joined the group of Doug Rees at Caltech to study nitrogenase, and re-turned to Germany in 2003 as a junior professor for Protein Crystallography in Göttingen. Since 2008 he is full professor of Biochemistry in Freiburg. Research in his group is focused on the structural and functional characterization of metalloproteins and integral membrane proteins.
©2012 by Walter de Gruyter Berlin Boston
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- No end in sight: the development of protein crystallography in Martinsried
- Highlight: No End in Sight: The Development of Protein Crystallography in Martinsried
- Functional and structural insights into astacin metallopeptidases
- β-Trefoil inhibitors – from the work of Kunitz onward
- Structural basis of the TAL effector–DNA interaction
- Nature’s way of handling a greenhouse gas: the copper-sulfur cluster of purple nitrous oxide reductase
- Rustless translation
- Structural basis of [NiFe] hydrogenase maturation by Hyp proteins
- Covalent and non-covalent reversible proteasome inhibition
- Structural origins of AGC protein kinase inhibitor selectivities: PKA as a drug discovery tool
- Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22
- N-terminal acetylation of annexin A2 is required for S100A10 binding
- Withaferin A binds covalently to the N-terminal domain of annexin A2
- PhoB transcriptional activator binds hierarchically to pho box promoters
- Research Articles/Short Communications
- Protein Structure and Function
- Biochemical and functional characterization of human phospholipid scramblase 4 (hPLSCR4)
- Cell Biology and Signaling
- Dual-specificity phosphatases are targets of the Wnt/β-catenin pathway and candidate mediators of β-catenin/Ras signaling interactions
- Proteolysis
- Inhibition of Aeromonas sobria serine protease (ASP) by α2-macroglobulin
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- No end in sight: the development of protein crystallography in Martinsried
- Highlight: No End in Sight: The Development of Protein Crystallography in Martinsried
- Functional and structural insights into astacin metallopeptidases
- β-Trefoil inhibitors – from the work of Kunitz onward
- Structural basis of the TAL effector–DNA interaction
- Nature’s way of handling a greenhouse gas: the copper-sulfur cluster of purple nitrous oxide reductase
- Rustless translation
- Structural basis of [NiFe] hydrogenase maturation by Hyp proteins
- Covalent and non-covalent reversible proteasome inhibition
- Structural origins of AGC protein kinase inhibitor selectivities: PKA as a drug discovery tool
- Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22
- N-terminal acetylation of annexin A2 is required for S100A10 binding
- Withaferin A binds covalently to the N-terminal domain of annexin A2
- PhoB transcriptional activator binds hierarchically to pho box promoters
- Research Articles/Short Communications
- Protein Structure and Function
- Biochemical and functional characterization of human phospholipid scramblase 4 (hPLSCR4)
- Cell Biology and Signaling
- Dual-specificity phosphatases are targets of the Wnt/β-catenin pathway and candidate mediators of β-catenin/Ras signaling interactions
- Proteolysis
- Inhibition of Aeromonas sobria serine protease (ASP) by α2-macroglobulin
