Carbon-13 NMR studies of the influence of axial ligand orientation on haem electronic structure
- Citation:
- Turner, DL, Salgueiro CA, Schenkels P, Legall J, Xavier AV. 1995. Carbon-13 NMR studies of the influence of axial ligand orientation on haem electronic structure. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1246(1):24-28.
Abstract:
Three-quarters of the carbon-13 resonances of nuclei attached to the four haems of Desulfovibrio vulgaris ferricytochrome c3 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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