[A covalently linked complex of cytochrome P-450 with adrenodoxin. Localization of the adrenodoxin binding site of cytochrome P-450].

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Title[A covalently linked complex of cytochrome P-450 with adrenodoxin. Localization of the adrenodoxin binding site of cytochrome P-450].
Publication TypeJournal Article
Year of Publication1988
AuthorsTurko, IV, Adamovich, TB, Kirillova, NM, Usanov, SA, Chashchin, VL
JournalBiokhimiia
Volume53
Issue11
Pagination1810-6
Date Published1988 Nov
ISSN0320-9725
KeywordsAdrenodoxin, Amino Acid Sequence, Binding Sites, Cross-Linking Reagents, Cytochrome P-450 Enzyme System, Molecular Sequence Data
Abstract

Cytochrome P-450scc and adrenodoxin were cross-linked with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. The sample containing 94% of a cross-linked complex and 6% of free cytochrome P-450scc was obtained after purification on cholate-Sepharose. Cytochrome P-450scc in the cross-linked complex is not reduced in the presence of NADPH and adrenodoxin reductase, but completely preserves its high spin form in the presence of Tween-20 or pregnenolone. The use of radioactive labelled adrenodoxin, chemical cleavage of cytochrome P-450scc from the cross-linked complex by o-iodosobenzoic acid and HPLC for separation of peptides demonstrated that the cytochrome P-450scc complex with adrenodoxin was cross-linked through two amino acid sequences of cytochrome P-450scc, i.e., Leu 88-Trp108 and Leu368-Trp417.

Alternate JournalBiokhimiia
PubMed ID3251548