Molybdenum-containing nitrite reductases: Spectroscopic characterization and redox mechanism

Wang, Jun; Keceli, Gizem; Cao, Rui; Su, Jiangtao; Mi, Zhiyuan

doi:10.1080/13510002.2016.1206175

Cited by 22 publications

(16 citation statements)

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“…All five molybdoenzymes in plants (nitrate reductase, xanthine oxidase reductase (XOR), aldehyde oxidase (AO), sulfite oxidase (SO), and mARC) are able to catalyze the one-electron reduction of nitrite to NO. The molybdoenzymes are classified depending on how Moco binds to the enzyme’s active site: either covalently through an enzyme cysteine thiol group (NR, SO, and mARC) or with inorganic sulfur (XOR and AO) [55,56]. All of these enzymes show nitrite reductase activity to produce NO in vitro and in anaerobic conditions [44].…”

Section: Does Nr Catalyze Nitrite Reduction To No?mentioning

confidence: 99%

“…All of these enzymes show nitrite reductase activity to produce NO in vitro and in anaerobic conditions [44]. The four known human molybdenum-containing enzymes are the same as those in plants, except for NR, and they can also function as nitrite reductases under hypoxic conditions [56]. In mammals, two known pathways for NO formation are known: arginine oxidation under normoxic or aerobic conditions and nitrite reduction during hypoxia or anaerobiosis [56].…”

Section: Does Nr Catalyze Nitrite Reduction To No?mentioning

confidence: 99%

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Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Tejada‐Jiménez

Llamas

Galván

et al. 2019

Plants

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Nitric oxide is a gaseous secondary messenger that is critical for proper cell signaling and plant survival when exposed to stress. Nitric oxide (NO) synthesis in plants, under standard phototrophic oxygenic conditions, has long been a very controversial issue. A few algal strains contain NO synthase (NOS), which appears to be absent in all other algae and land plants. The experimental data have led to the hypothesis that molybdoenzyme nitrate reductase (NR) is the main enzyme responsible for NO production in most plants. Recently, NR was found to be a necessary partner in a dual system that also includes another molybdoenzyme, which was renamed NO-forming nitrite reductase (NOFNiR). This enzyme produces NO independently of the molybdenum center of NR and depends on the NR electron transport chain from NAD(P)H to heme. Under the circumstances in which NR is not present or active, the existence of another NO-forming system that is similar to the NOS system would account for NO production and NO effects. PII protein, which senses and integrates the signals of the C–N balance in the cell, likely has an important role in organizing cell responses. Here, we critically analyze these topics.

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Section: Does Nr Catalyze Nitrite Reduction To No?mentioning

confidence: 99%

Section: Does Nr Catalyze Nitrite Reduction To No?mentioning

confidence: 99%

Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Tejada‐Jiménez

Llamas

Galván

et al. 2019

Plants

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“…(2) ) that is predicted to prevent NO export [15] , [26] , [27] , [28] , [29] , [30] , [31] . It should also be noted that several other enzymes besides Hb have been proposed as physiological nitrite reductases [32] , [33] , [34] , [35] , [36] , [37] , [38] , [39] , [40] , [41] , [42] , [43] , [44] , including some found in RBCs. However, our work confirms the role of Hb as the primary erythrocytic nitrite reductase [45] .…”

Section: Introductionmentioning

confidence: 99%

Erythrocytic bioactivation of nitrite and its potentiation by far-red light

et al. 2019

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BackgroundNitrite is reduced by heme-proteins and molybdenum-containing enzymes to form the important signaling molecule nitric oxide (NO), mediating NO signaling. Substantial evidence suggests that deoxygenated hemoglobin within red blood cells (RBCs) is the main erythrocytic protein responsible for mediating nitrite-dependent NO signaling. In other work, infrared and far red light have been shown to have therapeutic potential that some attribute to production of NO. Here we explore whether a combination of nitrite and far red light treatment has an additive effect in NO-dependent processes, and whether this effect is mediated by RBCs.Methods and resultsUsing photoacoustic imaging in a rat model as a function of varying inspired oxygen, we found that far red light (660 nm, five min. exposure) and nitrite feeding (three weeks in drinking water at 100 mg/L) each separately increased tissue oxygenation and vessel diameter, and the combined treatment was additive. We also employed inhibition of human platelet activation measured by flow cytometry to assess RBC-dependent nitrite bioactivation and found that far red light dramatically potentiates platelet inhibition by nitrite. Blocking RBC-surface thiols abrogated these effects of nitrite and far-red light. RBC-dependent production of NO was also shown to be enhanced by far red light using a chemiluminescence-based nitric oxide analyzer. In addition, RBC-dependent bioactivation of nitrite led to prolonged lag times for clotting in platelet poor plasma that was enhanced by exposure to far red light.ConclusionsOur results suggest that nitrite leads to the formation of a photolabile RBC surface thiol-bound species such as an S-nitrosothiol or heme-nitrosyl (NO-bound heme) for which far red light enhances NO signaling. These findings expand our understanding of RBC-mediated NO production from nitrite. This pathway of NO production may have therapeutic potential in several applications including thrombosis, and, thus, warrants further study.

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“…Furthermore, nitrite reduction is an important biochemical process associated with, for example, neurotransmission, immune response and apoptosis in various organisms . Soil bacteria metabolise nitrite to NO by means of nitrite reductases, which are enzymes of the EC 1.7 group with iron‐, copper‐ or molybdenum‐based active centres. Both NO and N 2 O, which is another product of biological nitrite reduction, are greenhouse gases that also participate in the destruction of the ozone layer.…”

Section: Introductionmentioning

confidence: 99%

Nitrite Reduction in Aqueous Solution Mediated by Amavadin Homologues: N₂O Formation and Water Oxidation

Dias

Bekhti

Kuznetsov

et al. 2018

Chemistry A European J

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Reactions of two vanadium(IV) complex anions that are homologues of amavadin, [V(HIDPA) ] and [V(HIDA) ] (HIDPA=N-oxyiminodipropionate, HIDA=N-oxyiminodiacetate), with the nitrite ion (NO ) in aqueous solution were investigated by experimental (absorption spectroscopy in the visible range, through measurements of dioxygen formed in solution from water oxidation and identification of nitrogen oxide species of a gaseous atmosphere from nitrite reduction by using an IR analyser) and theoretical methods. Two reactions, mediated by the vanadium complexes, with environmental and biological significance, were observed in this system, namely, reduction of nitrite to N O and oxidation of water to molecular oxygen. The reduction of nitrite, as studied by DFT calculations, occurs through the formation of NO (ΔG =14.3 kcal mol ), which is strongly dependent on pH and slightly endergonic, and is then easily converted into N O, with an overall activation barrier of ΔG =11.8 kcal mol . The later process includes dimerisation of NO assisted by one molecule of the V complex, protonation and oxidation of the formed ONNO ligand by another amavadin molecule or by nitrite, and NO bond cleavage/proton transfer in the ONNOH ligand. The results indicate that amavadin exhibits an unusual nitrite reductase type activity that could be involved in nitrogen metabolism of Amanita muscaria and other fungi containing this vanadium complex.

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Molybdenum-containing nitrite reductases: Spectroscopic characterization and redox mechanism

Abstract: To fully understand the catalytic mechanisms of these physiologically/pathologically important nitrite reductases, structural studies on substrate-redox center interaction are needed.

Cited by 22 publications

References 84 publications

Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Erythrocytic bioactivation of nitrite and its potentiation by far-red light

Nitrite Reduction in Aqueous Solution Mediated by Amavadin Homologues: N₂O Formation and Water Oxidation

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Molybdenum-containing nitrite reductases: Spectroscopic characterization and redox mechanism

Abstract: To fully understand the catalytic mechanisms of these physiologically/pathologically important nitrite reductases, structural studies on substrate-redox center interaction are needed.

Cited by 22 publications

References 84 publications

Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Erythrocytic bioactivation of nitrite and its potentiation by far-red light

Nitrite Reduction in Aqueous Solution Mediated by Amavadin Homologues: N2O Formation and Water Oxidation

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Nitrite Reduction in Aqueous Solution Mediated by Amavadin Homologues: N₂O Formation and Water Oxidation