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Higher blood flow and circulating NO products offset high-altitude hypoxia among Tibetans.
Erzurum SC, Ghosh S, Janocha AJ, Xu W, Bauer S, Bryan NS, Tejero J, Hemann C, Hille R, Stuehr DJ, Feelisch M, Beall CM. Erzurum SC, et al. Among authors: hemann c. Proc Natl Acad Sci U S A. 2007 Nov 6;104(45):17593-8. doi: 10.1073/pnas.0707462104. Epub 2007 Oct 30. Proc Natl Acad Sci U S A. 2007. PMID: 17971439 Free PMC article.
A conserved tryptophan in nitric oxide synthase regulates heme-dioxy reduction by tetrahydrobiopterin.
Wang ZQ, Wei CC, Ghosh S, Meade AL, Hemann C, Hille R, Stuehr DJ. Wang ZQ, et al. Among authors: hemann c. Biochemistry. 2001 Oct 30;40(43):12819-25. doi: 10.1021/bi011182s. Biochemistry. 2001. PMID: 11669618
In nitric oxide synthase (NOS), (6R)-tetrahydrobiopterin (H(4)B) binds near the heme and can reduce a heme-dioxygen intermediate (Fe(II)O(2)) during Arg hydroxylation [Wei, C.-C., Wang, Z.-Q., Wang, Q., Meade, A. L., Hemann, C., Hille, R., and Stuehr, …
In nitric oxide synthase (NOS), (6R)-tetrahydrobiopterin (H(4)B) binds near the heme and can reduce a heme-dioxygen intermediate (Fe(II)O(2) …
Structure of tetrahydrobiopterin tunes its electron transfer to the heme-dioxy intermediate in nitric oxide synthase.
Wei CC, Wang ZQ, Arvai AS, Hemann C, Hille R, Getzoff ED, Stuehr DJ. Wei CC, et al. Among authors: hemann c. Biochemistry. 2003 Feb 25;42(7):1969-77. doi: 10.1021/bi026898h. Biochemistry. 2003. PMID: 12590583
Previous work with the oxygenase domain of inducible NOS (iNOSoxy) demonstrated that H(4)B radical formation is kinetically coupled to disappearance of an initial heme-dioxy intermediate and to Arg hydroxylation in a single turnover reaction run at 10 degrees C [Wei, C …
Previous work with the oxygenase domain of inducible NOS (iNOSoxy) demonstrated that H(4)B radical formation is kinetically coupled to disap …
60 results