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Insights into properties and energetics of iron-sulfur proteins from simple clusters to nitrogenase
KTH, Superseded Departments, Biotechnology.
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2002 (English)In: Current opinion in chemical biology, ISSN 1367-5931, E-ISSN 1879-0402, Vol. 6, no 2, 259-273 p.Article, review/survey (Refereed) Published
Abstract [en]

Some of the principal physical features of iron-sulfur clusters in proteins are analyzed, including metal-ligand covalency, spin polarization, spin coupling, valence delocalization, valence interchange and small reorganization energies, with emphasis on recent spectroscopic and theoretical work. The current state of structural, spectroscopic, and computational knowledge for the iron-sulfur clusters in the nitrogenase iron and iron-molybdenum proteins is examined by comparison and contrast to 'simpler' iron-sulfur clusters. The differing interactions of the nitrogenase iron and iron-molybdenum clusters compared with those of other iron-sulfur clusters with the protein and solvent environment are also explored.

Place, publisher, year, edition, pages
2002. Vol. 6, no 2, 259-273 p.
Keyword [en]
azotobacter-vinelandii nitrogenase, hyperfine coupling-constants, density-functional theory, ferrous fe4s4 cluster, spin-state energies, electron-transfer, femo-cofactor, mofe protein, redox potentials, clostridium-pasteurianum
URN: urn:nbn:se:kth:diva-21445ISI: 000174821700021OAI: diva2:340143
QC 20100525Available from: 2010-08-10 Created: 2010-08-10Bibliographically approved

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