Nitric Oxide Synthesis Capabilities of Cytochrome P450 1A2 and NADPH-Cytochrome P450 Reductase from N^G-Hydroxy-L-Arginine
NO was formed from <I>N</I><SUP><I>G</I></SUP>-hydroxy-<FONT SIZE=-2>L</FONT>-arginine by cytochrome P450 1A2 (P450 1A2) with turnover numbers of 0.6 - 1.2 nmol/nmolP450/min and 62 pmol/nmolP450/min in peroxide-supported shunt and reconstituted systems, respectively. A Glu318Ala mutation of P450 1A2 enhanced the shunt-reaction activity up to 7.3-fold, whereas the mutation abolished the activity with the reconstituted system. Involvement of H<SUB>2</SUB>O<SUB>2</SUB> or superoxide anion in the NO synthesis is also suggested.
- Chemistry letters
Chemistry letters 1997(8), 759-760, 1997-08
The Chemical Society of Japan