Title : Determination of haem electronic structure in His-Met cytochromes c by 13C-NMR. The effect of the axial ligands.

Pub. Date : 1995 Feb 1

PMID : 7867644






1 Functional Relationships(s)
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1 A comparison between the orientation of the rhombic perturbations and the crystal structures of horse cytochrome c and P. aeruginosa cytochrome c551 reveals that the orientation of the histidine and methionine axial ligands dominates the rhombic perturbation and that the two ligands have approximately equal influence. Histidine cytochrome c, somatic Equus caballus