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A pivotal role for tryptophan 447 in enzymatic coupling of human endothelial nitric oxide synthase (eNOS): effects on tetrahydrobiopterin-dependent catalysis and eNOS dimerization.

Abstract:

Tetrahydrobiopterin (BH4) is a required cofactor for the synthesis of NO by NOS. Bioavailability of BH4 is a critical factor in regulating the balance between NO and superoxide production by endothelial NOS (eNOS coupling). Crystal structures of the mouse inducible NOS oxygenase domain reveal a homologous BH4-binding site located in the dimer interface and a conserved tryptophan residue that engages in hydrogen bonding or aromatic stacking interactions with the BH4 ring. The role of this resi...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m113.493023

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Journal:
The Journal of biological chemistry
Volume:
288
Issue:
41
Pages:
29836-29845
Publication date:
2013-10-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:d525a072-70ad-4d39-9924-f1d75fc2ee98
Source identifiers:
418604
Local pid:
pubs:418604

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