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Topological chirality of iron-sulfur proteins

Biopolymers, 1997
An examination of x-ray structures of single-cluster [4Fe-4S] proteins in the Protein Data Bank has revealed that all redox proteins and the glutamine 5-phosphoribosyl-l-pyrophosphate amidotransferase from Bacillus subtilis have a topological configuration arbitrarily designated as D, whereas the DNA repair enzyme endonuclease III from Escherichia coli
C, Liang, K, Mislow
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Iron–sulfur protein folds, iron–sulfur chemistry, and evolution

JBIC Journal of Biological Inorganic Chemistry, 2007
An inventory of unique local protein folds around Fe-S clusters has been derived from the analysis of protein structure databases. Nearly 50 such folds have been identified, and over 90% of them harbor low-potential [2Fe-2S](2+,+) or [4Fe-4S](2+,+) clusters. In contrast, high-potential Fe-S clusters, notwithstanding their structural diversity, occur in
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IRON-SULFUR PROTEINS

Chemical & Engineering News Archive, 2000
Adecade ago, bioinorganic chemists thought they had pretty much figured out what the iron-sulfur clusters found in many proteins were there for. The prevailing wisdom was that these proteins had one basic function in biology—to move electrons around, says Michael K. Johnson, chemistry professor at the University of Georgia, Athens. Biological processes
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Iron-Sulfur Proteins

2007
The sections in this article are 1 Introduction 2 NMR and Hyperfine Coupling in Various FeS Proteins 3 Structural Information on the Diamagnetic Part 4 Biographical Sketches Related ...
BERTINI, IVANO, LUCHINAT, CLAUDIO
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Folding properties of iron—sulfur proteins

Inorganica Chimica Acta, 1998
Abstract The 1 H NMR spectra in water of HiPIP I from Ectothiorhodospira halophila , the Cys77Ser mutant of the HiPIP from Chromatium vinosum , the 7Fe8S ferredoxin from Bacillus schlegelii , the 8Fe8S ferredoxin from Clostridium pasteurianum and the 2Fe2S ferredoxin from P.
BERTINI, IVANO   +3 more
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