Title : Inhibition of electron transfer from adrenodoxin to cytochrome P-450scc by chemical modification with pyridoxal 5'-phosphate: identification of adrenodoxin-binding site of cytochrome P-450scc.

Pub. Date : 1989 Aug 22

PMID : 2819041






2 Functional Relationships(s)
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1 Covalent modification of cytochrome P-450scc (purified from bovine adrenocortical mitochondria) with pyridoxal 5"-phosphate (PLP) was found to cause inhibition of the electron-accepting ability of this enzyme from its physiological electron donor, adrenodoxin, without conversion to the "P-420" form. Pyridoxal Phosphate cholesterol side-chain cleavage enzyme, mitochondrial Bos taurus
2 Covalent modification of cytochrome P-450scc (purified from bovine adrenocortical mitochondria) with pyridoxal 5"-phosphate (PLP) was found to cause inhibition of the electron-accepting ability of this enzyme from its physiological electron donor, adrenodoxin, without conversion to the "P-420" form. Pyridoxal Phosphate cholesterol side-chain cleavage enzyme, mitochondrial Bos taurus