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Abstract
Three-quarters of the carbon-13 resonances of nuclei attached to the four haems of Desulfovibrio uulgaris ferricytochrome c 3 are assigned. Preliminary analysis of their Fermi contact interactions shows that the shifts are directly related to the orientation of both of the axial histidine ligands in each case and the approach can therefore be used to obtain structural information in other cytochromes with bis-histidinyl coordination. The implications for the control of redox potential in cytochromes are discussed.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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