Abstract
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.
MeSH terms
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Animals
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Cyanides / metabolism
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Cytochrome c Group / analogs & derivatives*
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Cytochrome c Group / metabolism
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Cytochromes c*
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Dimethyl Sulfoxide
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Imidazoles / metabolism
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Iron / metabolism*
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Ligands
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Macromolecular Substances
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Myoglobin / metabolism
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Protein Binding
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Spectrophotometry, Infrared
Substances
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Cyanides
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Cytochrome c Group
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Imidazoles
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Ligands
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Macromolecular Substances
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Myoglobin
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dicarboxymethyl-cytochrome c
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imidazole
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Cytochromes c
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Iron
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Dimethyl Sulfoxide