NDLI: Exploring the electron transfer properties of neuronal nitric-oxide synthase by reversal of the FMN redox potential.

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Exploring the electron transfer properties of neuronal nitric-oxide synthase by reversal of the FMN redox potential.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Li, Huiying Sligar, Stephen G. Poulos, Thomas L. Das, Aditi Jamal, Joumana Sibhatu, Hiruy
Description	Author Affiliation: Li H ( Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697, USA.)
Abstract	In nitric-oxide synthase (NOS) the FMN can exist as the fully oxidized (ox), the one-electron reduced semiquinone (sq), or the two-electron fully reduced hydroquinone (hq). In NOS and microsomal cytochrome P450 reductase the sq/hq redox potential is lower than that of the ox/sq couple, and hence it is the hq form of FMN that delivers electrons to the heme. Like NOS, cytochrome P450BM3 has the FAD/FMN reductase fused to the C-terminal end of the heme domain, but in P450BM3 the ox/sq and sq/hq redox couples are reversed, so it is the sq that transfers electrons to the heme. This difference is due to an extra Gly residue found in the FMN binding loop in NOS compared with P450BM3. We have deleted residue Gly-810 from the FMN binding loop in neuronal NOS (nNOS) to give Delta G810 so that the shorter binding loop mimics that in cytochrome P450BM3. As expected, the ox/sq redox potential now is lower than the sq/hq couple. Delta G810 exhibits lower NO synthase activity but normal levels of cytochrome c reductase activity. However, unlike the wild-type enzyme, the cytochrome c reductase activity of Delta G810 is insensitive to calmodulin binding. In addition, calmodulin binding to Delta G810 does not result in a large increase in FMN fluorescence as in wild-type nNOS. These results indicate that the FMN domain in Delta G810 is locked in a unique conformation that is no longer sensitive to calmodulin binding and resembles the 'on' output state of the calmodulin-bound wild-type nNOS with respect to the cytochrome c reduction activity.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	50
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-12-12
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Flavin Mononucleotide Chemistry Neurons Metabolism Nitric Oxide Synthase Type I Oxidation-Reduction Animals Biochemistry Calmodulin Models, Chemical Models, Molecular Molecular Conformation NADPH-Ferrihemoprotein Reductase Protein Binding Spectrometry, Fluorescence Time Factors Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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