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Spectroscopic studies on two-iron ferredoxins

Published online by Cambridge University Press:  17 March 2009

R. H. Sands  and
W. R. Dunham
R. H. Sands
Affiliation:
Department of Physics and Biophysics Research Division, University of Michzgan, Ann Arbor, MI 48104 U.S.A.
W. R. Dunham
Affiliation:
Department of Physics and Biophysics Research Division, University of Michzgan, Ann Arbor, MI 48104 U.S.A.
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Extract

The application of magnetic resonance techniques to biological systems has permitted a detailed study of the nature of the active sites of many proteins that had not been possible previously. Among these is the whole class of iron—sulphur proteins which have been implicated as electron transport proteins in a variety of fundamental processes: photosynthesis, hydroxylation and nitrogen fixation to name but a few.

The single-iron proteins in this class, the rubredoxins, have been studied extensively by chemical, spectroscopic and X-ray crystallographic techniques (Lovenberg, 1973), and the active site is composed of a single iron atom bound in a distorted tetrahedron of cysteine sulphur ligands. The iron is high-spin ferric in the oxidized state and high-spin ferrous in the reduced state. This structure is shown in Fig. I (α).

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 7 , Issue 4 , November 1974 , pp. 443 - 504
Copyright
Copyright © Cambridge University Press 1974

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