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- W1996220108 abstract "Cobalt-substituted cytochrome P450cam was recently reconstituted by Wagner et al (J. Biol. Chem. 256, 6266, (1981)). A model of its coordination site was constructed to determine the mode of axial coordination of the native enzyme. Complexes were prepared from cobalt porphyrins (cobalt-protoporphyrin IX (CoPPIX), cobalt-meso-tetraphenylporphyrin, cobalt-γ-laurylpyridyl triphenylporphyrin, and cobalt-octaethylporphyrin), thioglycolate ester, and tetramethylammonium hydroxide in organic solvents. Complexes prepared in an organic solvent such as CHC13 under air at room temperature exhibited a stable Soret hyperporphyrin spectrum characterized by split Soret bands, especially like that of the thiol-Co-P450cam complex Comparison of the spectra of the hyperporphyrin spectral complexes titrated with various types of alcohol and imidazole, with the spectrum of Co-P450cam in the oxidized state support the idea that an axial thiolate at the fifth position and a hydroxyl group of alcohol at the sixth position of the heme form the coordination site of Co-P450cam The CoPPIX-thiolate-ethanol complex retaining S−-Co(III)-OH coordination is thought to be a possible model of Co-P450cam in the oxidized state." @default.
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- W1996220108 date "1986-01-01" @default.
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- W1996220108 title "Model of the coordination site for cobalt-substituted cytochrome P450cam" @default.
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- W1996220108 doi "https://doi.org/10.1016/0162-0134(86)80036-8" @default.
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