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

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.[1]

References

  1. Formation and properties of a stable 'high-potential' copper-iron-sulphur cluster in a ferredoxin. Butt, J.N., Niles, J., Armstrong, F.A., Breton, J., Thomson, A.J. Nat. Struct. Biol. (1994) [Pubmed]
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