Sulfite oxidase catalyzes single electron transfer at molybdenum domain to reduce nitrite to nitric oxide

Wang, Jun; Krizowski, Sabina; Fischer, Katrin; Niks, Dimitri; Tejero, Jesús; Sparacino-Watkins, Courtney; Wang, Ling; Ragireddy, Venkata; Frizzell, Sheila; Kelley, Eric E.; Zhang, Yingze; Basu, Partha; Hille, Russ; Schwarz, Guenter; Gladwin, Mark T.

doi:10.1016/j.niox.2014.09.146

Cited by 7 publications

(14 citation statements)

References 40 publications

(59 reference statements)

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“…This can be interpreted as a direct reaction of nitrous acid with the heme, as previously proposed (31,33). Xanthine oxidase and aldehyde oxidase do not show this direct relationship between rate and proton concentration, although lower pH does increase the rate of the reaction (19,21,34,35). mARC-1 exhibited a similarly limited change in the reaction rates, with only a 3-fold change in rate at pH 7.4 versus 6.4 (Fig.…”

Section: Effect Of Ph On No Formationmentioning

confidence: 92%

Nitrite Reductase and Nitric-oxide Synthase Activity of the Mitochondrial Molybdopterin Enzymes mARC1 and mARC2

Sparacino-Watkins

Tejero

Sun

et al. 2014

Journal of Biological Chemistry

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153

139

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Background: Nitrite reduction pathways are critical for biological NO production under hypoxia. Results: The mitochondrial enzyme mARC reduces nitrite to NO using cytochrome b 5 as electron donor. Conclusion: mARC forms an electron transfer chain with NADH, cytochrome b 5 , and cytochrome b 5 reductase to reduce nitrite to NO. Significance: mARC proteins may constitute a new pathway for hypoxic NO production in vivo.

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Section: Effect Of Ph On No Formationmentioning

confidence: 92%

Nitrite Reductase and Nitric-oxide Synthase Activity of the Mitochondrial Molybdopterin Enzymes mARC1 and mARC2

Sparacino-Watkins

Tejero

Sun

et al. 2014

Journal of Biological Chemistry

Self Cite

153

139

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“…Accordingly, several reports highlight a role for nitritederived NO in cytoprotection during hypoxia in mammals (52). The underlying mechanisms are still under investigation, but several enzymes involved in nitrate-to-nitrite reduction and nitrite-to-NO reduction have been identified, such as xanthine oxidoreductase (53), deoxyhemoglobin (51), and sulfite oxidase (54). Similar to fish, algae and land plants frequently face hypoxic or anaerobic conditions in their natural habitats.…”

Section: +mentioning

confidence: 99%

Occurrence, structure, and evolution of nitric oxide synthase–like proteins in the plant kingdom

et al. 2016

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Nitric oxide (NO) signaling regulates various physiological processes in both animals and plants. In animals, NO synthesis is mainly catalyzed by NO synthase (NOS) enzymes. Although NOS-like activities that are sensitive to mammalian NOS inhibitors have been detected in plant extracts, few bona fide plant NOS enzymes have been identified. We searched the data set produced by the 1000 Plants (1KP) international consortium for the presence of transcripts encoding NOS-like proteins in over 1000 species of land plants and algae. We also searched for genes encoding NOS-like enzymes in 24 publicly available algal genomes. We identified no typical NOS sequences in 1087 sequenced transcriptomes of land plants. In contrast, we identified NOS-like sequences in 15 of the 265 algal species analyzed. Even if the presence of NOS enzymes assembled from multipolypeptides in plants cannot be conclusively discarded, the emerging data suggest that, instead of generating NO with evolutionarily conserved NOS enzymes, land plants have evolved finely regulated nitrate assimilation and reduction processes to synthesize NO through a mechanism different than that in animals.

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“…Although no "dedicated" nitrite reductase was ever found in mammals, numerous metalloproteins, present in cells to conduct other functions, were shown to be able to reduce nitrite to NO: (i) the molybdenum-containing enzymes xanthine oxidase/ xanthine dehydrogenase (XO/XD), 37−43 aldehyde oxidase (AO), 42,44 sulfite oxidase, 45 and mitochondrial amidoxime reducing component, 46 (ii) a growing number of heme-containing proteins, where hemoglobin and myoglobin 17,24,31,47,48 stand out in number of publications, but including also neuroglobin, 49 cytoglobin, 50 cytochrome c, 51 and cytochrome P 450 , 52,53 and (iii) several other proteins. 54−57 The nitrite "recycling" to NO is, however, a complex subject, overshadowed by the following main biochemical constraints.…”

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confidence: 99%

Nitrite Reductase Activity of Rat and Human Xanthine Oxidase, Xanthine Dehydrogenase, and Aldehyde Oxidase: Evaluation of Their Contribution to NO Formation in Vivo

et al. 2015

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Nitrite is presently considered a NO "storage form" that can be made available, through its one-electron reduction, to maintain NO formation under hypoxia/anoxia. The molybdoenzymes xanthine oxidase/dehydrogenase (XO/XD) and aldehyde oxidase (AO) are two of the most promising mammalian nitrite reductases, and in this work, we characterized NO formation by rat and human XO/XD and AO. This is the first characterization of human enzymes, and our results support the employment of rat liver enzymes as suitable models of the human counterparts. A comprehensive kinetic characterization of the effect of pH on XO and AO-catalyzed nitrite reduction showed that the enzyme's specificity constant for nitrite increase 8-fold, while the Km(NO2(-)) decrease 6-fold, when the pH decreases from 7.4 to 6.3. These results demonstrate that the ability of XO/AO to trigger NO formation would be greatly enhanced under the acidic conditions characteristic of ischemia. The dioxygen inhibition was quantified, and the Ki(O2) values found (24.3-48.8 μM) suggest that in vivo NO formation would be fine-tuned by dioxygen availability. The potential in vivo relative physiological relevance of XO/XD/AO-dependent pathways of NO formation was evaluated using HepG2 and HMEC cell lines subjected to hypoxia. NO formation by the cells was found to be pH-, nitrite-, and dioxygen-dependent, and the relative contribution of XO/XD plus AO was found to be as high as 50%. Collectively, our results supported the possibility that XO/XD and AO can contribute to NO generation under hypoxia inside a living human cell. Furthermore, the molecular mechanism of XO/AO-catalyzed nitrite reduction was revised.

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Sulfite oxidase catalyzes single electron transfer at molybdenum domain to reduce nitrite to nitric oxide

Cited by 7 publications

References 40 publications

Nitrite Reductase and Nitric-oxide Synthase Activity of the Mitochondrial Molybdopterin Enzymes mARC1 and mARC2

Nitrite Reductase and Nitric-oxide Synthase Activity of the Mitochondrial Molybdopterin Enzymes mARC1 and mARC2

Occurrence, structure, and evolution of nitric oxide synthase–like proteins in the plant kingdom

Nitrite Reductase Activity of Rat and Human Xanthine Oxidase, Xanthine Dehydrogenase, and Aldehyde Oxidase: Evaluation of Their Contribution to NO Formation in Vivo

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