Published June 2009
| Accepted Version + Supplemental Material
Journal Article
Open
Nanosecond photoreduction of inducible nitric oxide synthase by a Ru-diimine electron tunneling wire bound distant from the active site
Chicago
Abstract
A Ru-diimine wire, [(4,4′,5,5′-tetramethylbipyridine)_2Ru(F_9bp)]^(2+) (tmRu-F_9bp, where F_9bp is 4-methyl-4′-methylperfluorobiphenylbipyridine), binds tightly to the oxidase domain of inducible nitric oxide synthase (iNOSoxy). The binding of tmRu-F_9bp 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) × 10^7 s^(−1)) is fully seven orders of magnitude faster than the in vivo process.
Additional Information
© 2009 Elsevier. Received 3 December 2008; revised 1 April 2009; accepted 2 April 2009. Available online 17 April 2009. We thank Michael Marletta for the generous gift of protein reagents and for assistance with the iNOS purification protocol. This work was supported by NIH (DK19038 (H.B.G); GM070868 (H.B.G); GM068461 (J.R.W)), by the Fannie and John Hertz Foundation (A.R.D), the Ellison Medical Foundation (Senior Scholar Award in Aging to H.B.G), a NSF graduate research fellowship (C.A.W), and the Arnold and Mabel Beckman Foundation. Supplementary data associated with this article can be found, in the online version, at doi:10.1016/j.jinorgbio.2009.04.001.Attached Files
Accepted Version - nihms114634.pdf
Supplemental Material - Whitedmmc1.doc
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Additional details
- PMCID
- PMC2700734
- Eprint ID
- 15628
- Resolver ID
- CaltechAUTHORS:20090904-135737718
- NIH
- DK19038
- NIH
- GM070868
- NIH
- GM068461
- Fannie and John Hertz Foundation
- Ellison Medical Foundation
- NSF
- Arnold and Mabel Beckman Foundation
- Created
-
2009-09-23Created from EPrint's datestamp field
- Updated
-
2021-11-08Created from EPrint's last_modified field