Evolutionarily divergent electron donor proteins interact with P450MT2 through the same helical domain but different contact points

We have investigated the sites of N‐terminally truncated cytochrome P4501A1 targeted to mitochondria (P450MT2) which interact with adrenodoxin (Adx), cytochrome P450 reductase (CPR) and bacterial flavodoxin (Fln). The binding site was mapped by a combination of in vitro mutagenesis, in vivo screenin...

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Veröffentlicht in:	The EMBO journal 2001-05, Vol.20 (10), p.2394-2403
Hauptverfasser:	Anandatheerthavarada, Hindupur K., Amuthan, Govindasamy, Biswas, Gopa, Robin, Marie-Anne, Murali, Ramachandran, Waterman, Michael R., Avadhani, Narayan G.
Format:	Artikel
Sprache:	eng
Schlagworte:	adrenodoxin Adrenodoxin - metabolism Animals Binding Sites Cattle Chromosome Mapping Cross-Linking Reagents Cytochrome Cytochrome P-450 CYP1A1 - chemistry Cytochrome P-450 CYP1A1 - genetics Cytochrome P-450 CYP1A1 - metabolism cytochrome P450 cytochrome P450 reductase cytochrome P4501A1 cytochrome P450MT2 electron donor proteins electron transfer Enzymatic activity Evolution, Molecular flavodoxin Flavodoxin - metabolism Mammals Mitochondria, Liver - metabolism Models, Molecular Mutagenesis NADPH-Ferrihemoprotein Reductase - genetics NADPH-Ferrihemoprotein Reductase - metabolism P450 reductase Protein Structure, Secondary Proteins Rats Spectral analysis structural modeling Two-Hybrid System Techniques
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