The binding characteristics of the cytochrome c iron.
A comparison of the binding properties of myoglobin and cytochrome c shows that the latter, in the reduced state, has an unusually large affinity for ligands, including thioethers. This explains the outstanding stability of the methionine-iron bond of ferrous cytochrome c, and results from the intrinsic ability of the cytochrome c iron to delocalize its electrons into orbitals of the sixth axial ligand.
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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D000818:Animals; D003486:Cyanides / Q000378:metabolism; D003574:Cytochrome c Group / Q000031:analogs & derivatives* / Q000378:metabolism; D045304:Cytochromes c; D004121:Dimethyl Sulfoxide; D007093:Imidazoles / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D008024:Ligands; D046911:Macromolecular Substances; D009211:Myoglobin / Q000378:metabolism; D011485:Protein Binding; D013055:Spectrophotometry, Infrared
D003486:Cyanides; D003574:Cytochrome c Group; D007093:Imidazoles; D008024:Ligands; D046911:Macromolecular Substances; D009211:Myoglobin; C057834:dicarboxymethyl-cytochrome c; C029899:imidazole; D045304:Cytochromes c; D007501:Iron; D004121:Dimethyl Sulfoxide