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Nitric oxide is an obligate bacterial nitrification intermediate produced by hydroxylamine oxidoreductase.

ABSTRACT: Ammonia (NH₃)-oxidizing bacteria (AOB) emit substantial amounts of nitric oxide (NO) and nitrous oxide (N₂O), both of which contribute to the harmful environmental side effects of large-scale agriculture. The currently accepted model for AOB metabolism involves NH₃ oxidation to nitrite (NO₂^-) via a single obligate intermediate, hydroxylamine (NH₂OH). Within this model, the multiheme enzyme hydroxylamine oxidoreductase (HAO) catalyzes the four-electron oxidation of NH₂OH to NO₂^- We provide evidence that HAO oxidizes NH₂OH by only three electrons to NO under both anaerobic and aerobic conditions. NO₂^- observed in HAO activity assays is a nonenzymatic product resulting from the oxidation of NO by O₂ under aerobic conditions. Our present study implies that aerobic NH₃ oxidation by AOB occurs via two obligate intermediates, NH₂OH and NO, necessitating a mediator of the third enzymatic step.

SUBMITTER: Caranto JD

PROVIDER: S-EPMC5547625 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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Nitric oxide is an obligate bacterial nitrification intermediate produced by hydroxylamine oxidoreductase.

Caranto Jonathan D JD Lancaster Kyle M KM

Proceedings of the National Academy of Sciences of the United States of America 20170717 31

Ammonia (NH3)-oxidizing bacteria (AOB) emit substantial amounts of nitric oxide (NO) and nitrous oxide (N2O), both of which contribute to the harmful environmental side effects of large-scale agriculture. The currently accepted model for AOB metabolism involves NH3 oxidation to nitrite (NO2-) via a single obligate intermediate, hydroxylamine (NH2OH). Within this model, the multiheme enzyme hydroxylamine oxidoreductase (HAO) cataly ...[more]

PMID: 28716929

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Project description:Melanoma patients experience inferior survival after biochemotherapy when their tumors contain numerous cells expressing the inducible isoform of NO synthase (iNOS) and elevated levels of nitrotyrosine, a product derived from NO. Although several lines of evidence suggest that NO promotes tumor growth and increases resistance to chemotherapy, it is unclear how it shapes these outcomes. Here we demonstrate that modulation of NO-mediated S-nitrosation of cellular proteins is strongly associated with the pattern of response to the anticancer agent cisplatin in human melanoma cells in vitro. Cells were shown to express iNOS constitutively, and to generate sustained nanomolar levels of NO intracellularly. Inhibition of NO synthesis or scavenging of NO enhanced cisplatin-induced apoptotic cell death. Additionally, pharmacologic agents disrupting S-nitrosation markedly increased cisplatin toxicity, whereas treatments favoring stabilization of S-nitrosothiols (SNOs) decreased its cytotoxic potency. Activity of the proapoptotic enzyme caspase-3 was higher in cells treated with a combination of cisplatin and chemicals that decreased NO/SNOs, whereas lower activity resulted from cisplatin combined with stabilization of SNOs. Constitutive protein S-nitrosation in cells was detected by analysis with biotin switch and reduction/chemiluminescence techniques. Moreover, intracellular NO concentration increased significantly in cells that survived cisplatin treatment, resulting in augmented S-nitrosation of caspase-3 and prolyl-hydroxylase-2, the enzyme responsible for targeting the prosurvival transcription factor hypoxia-inducible factor-1? for proteasomal degradation. Because activities of these enzymes are inhibited by S-nitrosation, our data thus indicate that modulation of intrinsic intracellular NO levels substantially affects cisplatin toxicity in melanoma cells. The underlying mechanisms may thus represent potential targets for adjuvant strategies to improve the efficacy of chemotherapy.

Dataset Information

Nitric oxide is an obligate bacterial nitrification intermediate produced by hydroxylamine oxidoreductase.

Publications

Nitric oxide is an obligate bacterial nitrification intermediate produced by hydroxylamine oxidoreductase.

Similar Datasets

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