| Literature DB >> 7664060 |
J N Butt1, J Niles, F A Armstrong, J Breton, A J Thomson.
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) respectively, with copper bound formally as Cu(I). Cyanide causes selective loss of copper and regeneration of the [3Fe-4S] reactant. The results demonstrate the chemical feasibility of CuFeS clusters and suggest that they could exist naturally in biological systems.Entities:
Mesh:
Substances:
Year: 1994 PMID: 7664060 DOI: 10.1038/nsb0794-427
Source DB: PubMed Journal: Nat Struct Biol ISSN: 1072-8368