NITRIC-OXIDE SYNTHESIS CAPABILITIES OF CYTOCHROME-P450 1A2 AND NADPH-CYTOCHROME P450 REDUCTASE FROM N-G-HYDROXY-L-ARGININE

Authors
SANO H SATO H SAGAMI I SHIMIZU T
Citation
H. Sano et al., NITRIC-OXIDE SYNTHESIS CAPABILITIES OF CYTOCHROME-P450 1A2 AND NADPH-CYTOCHROME P450 REDUCTASE FROM N-G-HYDROXY-L-ARGININE, Chemistry Letters, (8), 1997, pp. 759-760
Citations number
15
Categorie Soggetti
Chemistry
Journal title
Chemistry Letters → ACNP
ISSN journal
03667022
Issue
8
Year of publication
1997
Pages
759 - 760
Database
ISI
SICI code
0366-7022(1997):8<759:NSCOC1>2.0.ZU;2-X
Abstract
NO was formed from N-G-hydroxy-L-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, r espectively. A Glu318Ala mutation of P450 1A2 enhanced the shunt-react ion activity up to 7.3-fold, whereas the mutation abolished the activi ty with the reconstituted system. involvement of H2O2 or superoxide an ion in the NO synthesis is also suggested.