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J. Biol. Chem., Vol. 255, Issue 8, 3242-3244, 04, 1980
BH Huynh, JJ Moura, I Moura, TA Kent, J LeGall, AV Xavier and E Munck
The tetrameric form of a Desulfovibrio gigas ferredoxin, named Fd II,
mediates electron transfer between cytochrome c3 and sulfite reductase. We
have studied two stable oxidation states of this protein with Mossbauer
spectroscopy and electron paramagnetic resonance. We found 3 iron
atoms/monomer and a spin concentration of 0.9 spins/monomer for the
oxidized protein. Taken together, the EPR and Mossbauer data demonstrate
conclusively the presence of a spin-coupled structure containing 3 iron
atoms and labile sulfur. The Mossbauer data show also that this metal
center is structurally similar, if not identical, with the low potential
center of a ferredoxin from Azotobacter vinelandii, a novel cluster
described recently (Emptage, M.H., Kent, T.A., Huynh, B.H., Rawlings, J.,
Orme-Johnson, W.H., and Munck, E. (1980) J. Biol. Chem. 255, 1793-1796).
Evidence for a three-iron center in a ferredoxin from Desulfovibrio gigas. Mossbauer and EPR studies
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