Brain nitric oxide synthase is a biopterin- and flavin-containing multi-functional oxido-reductase.

Abstract:

:Brain nitric oxide synthase is a Ca2+/calmodulin-regulated enzyme which converts L-arginine into NO. Enzymatic activity of this enzyme essentially depends on NADPH and is stimulated by tetrahydrobiopterin (H4biopterin). We found that purified NO synthase contains enzyme-bound H4biopterin, explaining the enzymatic activity observed in the absence of added cofactor. Together with the finding that H4biopterin was effective at substoichiometrical concentrations, these results indicate that NO synthase essentially depends on H4biopterin as a cofactor which is recycled during enzymatic NO formation. We found that the purified enzyme also contains FAD, FMN and non-heme iron in equimolar amounts and exhibits striking activities, including a Ca2+/calmodulin-dependent NADPH oxidase activity, leading to the formation of hydrogen peroxide at suboptimal concentrations of L-arginine or H4biopterin.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Mayer B,John M,Heinzel B,Werner ER,Wachter H,Schultz G,Böhme E

doi

10.1016/0014-5793(91)81031-3

subject

Has Abstract

pub_date

1991-08-19 00:00:00

pages

187-91

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)81031-3

journal_volume

288

pub_type

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