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Formation and properties of a stable 'high-potential' copper-iron-sulphur cluster in a ferredoxin.

Abstract:

A ferredoxin isolated from Desulfovibrio africanus contains a [3Fe-4S] cluster that reversibly binds a copper atom, yielding a stable product with a greatly increased reduction potential. The reaction is readily detected in protein molecules adsorbed as a film on an electrode surface. Electron paramagnetic resonance (EPR) and magnetic circular dichroism (MCD) spectra of oxidized and reduced bulk solution products support their assignment as [Cu3Fe-4S]2+ (S = 1/2) and [Cu3Fe-4S]1+ (S = 2) resp...

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Publication status:
Published

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Publisher copy:
10.1038/nsb0794-427

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Nature structural biology
Volume:
1
Issue:
7
Pages:
427-433
Publication date:
1994-07-05
DOI:
ISSN:
1072-8368
URN:
uuid:39ed7591-6b34-4ac6-ba5a-db1fa536d495
Source identifiers:
44569
Local pid:
pubs:44569

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