The reactivity of cytochrome c with soft ligands.
The spectral changes caused by binding soft ligands to the cytochrome c iron and their correlation to ligand affinities support the hypothesis that the iron-methionine sulfur bond of this heme protein is enhanced by delocalization of the metal t2g electrons into the empty 3d orbitals of the ligand atom. These findings also explain the unique spectrum of cytochrome c in the far red.
Schejter
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Lady Davis Chair of Biochemistry, Sackler Institute of Molecular Medicine, Sackler Medical School, Tel Aviv University, Israel.
Plotkin
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Vig
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D000818:Animals; D001665:Binding Sites; D003574:Cytochrome c Group / Q000737:chemistry*; D006736:Horses; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008024:Ligands; D009206:Myocardium / Q000201:enzymology; D013053:Spectrophotometry
D003574:Cytochrome c Group; D007506:Iron-Sulfur Proteins; D008024:Ligands