NDLI: Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2.

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Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2.

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Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Basu, Partha Gladwin, Mark T. Merchant, Bonnie A. Sparacino-watkins, Courtney E. Gauthier, Marc C. Thomas, John Sun, Bin Wang, Jun Azarov, Ivan Tejero, Jesús Ragireddy, Venkata
Description	Author Affiliation: Sparacino-Watkins CE ( From the Vascular Medicine Institute, University of Pittsburgh, Pittsburgh, Pennsylvania 15261.)
Abstract	Mitochondrial amidoxime reducing component (mARC) proteins are molybdopterin-containing enzymes of unclear physiological function. Both human isoforms mARC-1 and mARC-2 are able to catalyze the reduction of nitrite when they are in the reduced form. Moreover, our results indicate that mARC can generate nitric oxide (NO) from nitrite when forming an electron transfer chain with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductase. The rate of NO formation increases almost 3-fold when pH was lowered from 7.5 to 6.5. To determine if nitrite reduction is catalyzed by molybdenum in the active site of mARC-1, we mutated the putative active site cysteine residue (Cys-273), known to coordinate molybdenum binding. NO formation was abolished by the C273A mutation in mARC-1. Supplementation of transformed Escherichia coli with tungsten facilitated the replacement of molybdenum in recombinant mARC-1 and abolished NO formation. Therefore, we conclude that human mARC-1 and mARC-2 are capable of catalyzing reduction of nitrite to NO through reaction with its molybdenum cofactor. Finally, expression of mARC-1 in HEK cells using a lentivirus vector was used to confirm cellular nitrite reduction to NO. A comparison of NO formation profiles between mARC and xanthine oxidase reveals similar Kcat and Vmax values but more sustained NO formation from mARC, possibly because it is not vulnerable to autoinhibition via molybdenum desulfuration. The reduction of nitrite by mARC in the mitochondria may represent a new signaling pathway for NADH-dependent hypoxic NO production.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	15
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-04-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Coenzymes Metabolism Metalloproteins Mitochondria Enzymology Mitochondrial Proteins Nitric Oxide Synthase Nitrite Reductases Oxidoreductases Pteridines Amino Acid Sequence Cytochrome Reductases Cytochromes B5 Electron Transport HEK293 Cells Hydrogen-Ion Concentration Kinetics Molecular Sequence Data Molybdenum Nitric Oxide Nitrites Oxygen Recombinant Proteins Sequence Homology, Amino Acid Xanthine Oxidase Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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