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(l). 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.
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Butt, J., Niles, J., Armstrong, F. et al. Formation and properties of a stable ‘high-potential’ copper-iron-sulphur cluster in a ferredoxin. Nat Struct Mol Biol 1, 427–433 (1994). https://doi.org/10.1038/nsb0794-427
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DOI: https://doi.org/10.1038/nsb0794-427
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