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 Lettjournal_title
FEBS lettersauthors
Mayer B,John M,Heinzel B,Werner ER,Wachter H,Schultz G,Böhme Edoi
10.1016/0014-5793(91)81031-3subject
Has Abstractpub_date
1991-08-19 00:00:00pages
187-91issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(91)81031-3journal_volume
288pub_type
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