- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1038/nsb0794-427
-
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- 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
- Copyright date:
- 1994
Journal article
Formation and properties of a stable 'high-potential' copper-iron-sulphur cluster in a ferredoxin.
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