Unknown

Dataset Information

0

Nanosecond photoreduction of inducible nitric oxide synthase by a Ru-diimine electron tunneling wire bound distant from the active site.


ABSTRACT: A Ru-diimine wire, [(4,4',5,5'-tetramethylbipyridine)2Ru(F9bp)]2+ (tmRu-F9bp, where F9bp is 4-methyl-4'-methylperfluorobiphenylbipyridine), binds tightly to the oxidase domain of inducible nitric oxide synthase (iNOSoxy). The binding of tmRu-F9bp is independent of tetrahydrobiopterin, arginine, and imidazole, indicating that the wire resides on the surface of the enzyme, distant from the active-site heme. Photoreduction of an imidazole-bound active-site heme iron in the enzyme-wire conjugate (k(ET) = 2(1) x 10(7) s(-1)) is fully seven orders of magnitude faster than the in vivo process.

SUBMITTER: Whited CA 

PROVIDER: S-EPMC2700734 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Nanosecond photoreduction of inducible nitric oxide synthase by a Ru-diimine electron tunneling wire bound distant from the active site.

Whited Charlotte A CA   Belliston-Bittner Wendy W   Dunn Alexander R AR   Winkler Jay R JR   Gray Harry B HB  

Journal of inorganic biochemistry 20090417 6


A Ru-diimine wire, [(4,4',5,5'-tetramethylbipyridine)2Ru(F9bp)]2+ (tmRu-F9bp, where F9bp is 4-methyl-4'-methylperfluorobiphenylbipyridine), binds tightly to the oxidase domain of inducible nitric oxide synthase (iNOSoxy). The binding of tmRu-F9bp is independent of tetrahydrobiopterin, arginine, and imidazole, indicating that the wire resides on the surface of the enzyme, distant from the active-site heme. Photoreduction of an imidazole-bound active-site heme iron in the enzyme-wire conjugate (k(  ...[more]

Similar Datasets

| S-EPMC6739416 | biostudies-literature
| S-EPMC2596599 | biostudies-literature
| S-EPMC7686262 | biostudies-literature
| S-EPMC5754034 | biostudies-literature
| S-EPMC4036732 | biostudies-literature
| S-EPMC4808502 | biostudies-literature
| S-EPMC3465397 | biostudies-literature
| S-EPMC2797321 | biostudies-literature
| S-EPMC2516252 | biostudies-literature
| S-EPMC3823503 | biostudies-literature