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Identification of the domains of neuronal nitric oxide synthase by limited proteolysis.

Abstract:

Nitric oxide synthase (EC 1.14.13.39) binds arginine and NADPH as substrates, and FAD, FMN, tetrahydrobiopterin, haem and calmodulin as cofactors. The protein consists of a central calmodulin-binding sequence flanked on the N-terminal side by a haem-binding region, analogous to cytochrome P-450, and on the C-terminal side by a region homologous with NADPH:cytochrome P-450 reductase. The structure of recombinant rat brain nitric oxide synthase was analysed by limited proteolyis. The products w...

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Publication status:
Published

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Riveros-Moreno, V More by this author
Moncada, S More by this author
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Journal:
The Biochemical journal
Volume:
314 ( Pt 1)
Issue:
1
Pages:
55-62
Publication date:
1996-02-05
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:12888b8f-3aa7-4720-8ad9-c78e02f5ae0a
Source identifiers:
72679
Local pid:
pubs:72679

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