Electron transfer reactions of Anabaena PCC 7119 ferredoxin:NADP+ reductase with nonphysiological oxidants

Anusevičius, Žilvinas; Martínez‐Júlvez, Marta; Genzor, Carlos G.; Nivinskas, Henrikas; Gómez‐Moreno, Carlos; Č≐nas, Narimantas

doi:10.1016/s0005-2728(97)00028-5

Cited by 35 publications

(42 citation statements)

References 37 publications

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“…Oxygen‐sensitive nitroreductases are found in Escherichia coli (Mason & Holtzman, 1975; Peterson et al , 1979) and several Clostridium strains (Angermaier & Simon, 1983). In addition, some enzymes like NADPH:cytochrome P450 reductase (Orna & Mason, 1989), ferredoxin:NADP + reductase (Anuseviĉius et al , 1997) and NADH:ubiquinone reductase (Bironaitè et al , 1991) also catalyze this type of reduction. The mammalian selenoprotein thioredoxin reductase also has nitroreductase activity either with one‐ or two‐electron chemistry, and the single‐electron reaction leads to superoxide anion formation (Ĉènas et al , 2006).…”

Section: Bacterial Nitroreductasesmentioning

confidence: 99%

Reduction of polynitroaromatic compounds: the bacterial nitroreductases

et al. 2008

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Most nitroaromatic compounds are toxic and mutagenic for living organisms, but some microorganisms have developed oxidative or reductive pathways to degrade or transform these compounds. Reductive pathways are based either on the reduction of the aromatic ring by hydride additions or on the reduction of the nitro groups to hydroxylamino and/or amino derivatives. Bacterial nitroreductases are flavoenzymes that catalyze the NAD(P)H-dependent reduction of the nitro groups on nitroaromatic and nitroheterocyclic compounds. Nitroreductases have raised a great interest due to their potential applications in bioremediation, biocatalysis, and biomedicine, especially in prodrug activation for chemotherapeutic cancer treatments. Different bacterial nitroreductases have been purified and their biochemical and kinetic parameters have been determined. The crystal structure of some nitroreductases have also been solved. However, the physiological role(s) of these enzymes remains unclear. Nitroreductase genes are widely spread within bacterial genomes, but are also found in archaea and some eukaryotic species. Although studies on regulation of nitroreductase gene expression are scarce, it seems that nitroreductase genes may be controlled by the MarRA and SoxRS regulatory systems that are involved in responses to several antibiotics and environmental chemical hazards and to specific oxidative stress conditions. This review covers the microbial distribution, types, biochemical properties, structure and regulation of the bacterial nitroreductases. The possible physiological functions and the biotechnological applications of these enzymes are also discussed.

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Section: Bacterial Nitroreductasesmentioning

confidence: 99%

Reduction of polynitroaromatic compounds: the bacterial nitroreductases

et al. 2008

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“…The reduction is mediated by single or two-electron system in the organisms. Singleelectron reduction reactions of nitro aromatic compounds are catalyzed by flavin containing reductases such as NADPH: cytochrome P-450 reductase, ferredoxin: NADP + reductase and bacterial oxygen-sensitive nitroreductases [5][6][7]. It was also well known that the two-electron reduction of nitro aromatic compounds to nitroso (NO) compounds and, subsequently, to hydroxylamines is specifically catalyzed by bacterial oxygen-insensitive nitroreductases [7,8].…”

Section: Introductionmentioning

confidence: 99%

Biotransformation of Nitro Aromatic Compounds by Flavin-Free NADHAzoreductase

Misal¹

2015

J Bioremed Biodeg

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Nitro aromatic compounds are the potential toxic organic pollutant released into the environment and are often resistant to degradation under normal environmental conditions. The biotransformation and/or detoxification of these compounds can be possible by microbial azoreductase enzyme. Azoreductase enzyme has an ability to reduce the toxic nitro group to corresponding amino group. In present report, the flavin-free NADH azoreductase was isolated and purified from alkaliphilic bacteria Bacillus badius. The enzyme was purified by a combination of ammonium sulphate precipitation and size exclusion chromatography. The purified azoreductase has efficiently demonstrated both azoreductase and nitroreductase activities. The biochemical properties of the azoreductase including cofactor requirement, substrate specificity and enzyme inhibition have been studied. The biotransformation of some selected nitro aromatic compounds like 3-nitro benzoic acid, 4-nitro toluene, 3-nitro toluene and 1-chloro-2-nitro benzene by purified azoreductase was carried out at 37°C. The reduction products of these nitro aromatic compounds were analyzed by IR and NMR spectroscopy.

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“…Although extensive literature exists on the mechanism of electron transfer between ferredoxin‐NADP + oxidoreductase and ferredoxin [5–12], relatively little is known about the mechanism of the single electron reduction of low‐molecular weight oxidants and redox active xenobiotics by ferredoxin‐NADP + oxidoreductase. The single electron reduction of quinones [13,14], viologen derivatives [15,16] and heteropentalenes [17] by ferredoxin‐NADP + oxidoreductase is supposed to be partly responsible for the herbicidal action of these compounds [16,17]. In addition to these compounds, nitroaromatics can undergo a single electron reduction by ferredoxin‐NADP + oxidoreductase [14,18].…”

Section: Introductionmentioning

confidence: 99%

“…The single electron reduction of quinones [13,14], viologen derivatives [15,16] and heteropentalenes [17] by ferredoxin‐NADP + oxidoreductase is supposed to be partly responsible for the herbicidal action of these compounds [16,17]. In addition to these compounds, nitroaromatics can undergo a single electron reduction by ferredoxin‐NADP + oxidoreductase [14,18]. Nitroaromatic compounds are widely used as industrial intermediate reagents in the production of dyes, rubbers, explosives and pharmaceuticals or are used as agrochemicals such as pesticides or veterinary drugs [19–21].…”

Section: Introductionmentioning

confidence: 99%

“…Up to now, attempts to define quantitative structure activity relationships (QSARs) for k cat as well as k cat / K m values for the reduction of various nitroaromatic compounds by flavoenzymes were unsuccessful [14,18,22,24]. Recently, however, we have described a QSAR for the two electron reduction of a series of nitrobenzimidazol(on)es by DT‐diaphorase based on calculated energy of the lowest unoccupied molecular orbital (E(LUMO)) [23].…”

Section: Introductionmentioning

confidence: 99%

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Quantitative structure activity relationships for the electron transfer reactions of Anabaena PCC 7119 ferredoxin‐NADP⁺ oxidoreductase with nitrobenzene and nitrobenzimidazolone derivatives: mechanistic implications

et al. 1999

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The steady state single electron reduction of polynitroaromatics by ferredoxin-NADP + oxidoreductase (EC 1.18.1.2) from cyanobacterium Anabaena PCC 7119 has been studied and quantitative structure activity relationships are described. The solubility of the polynitroaromatics as well as their reactivity towards ferredoxin-NADP oxidoreductase are markedly higher than those for previously studied mononitroaromatics and this enabled the independent measurement of the kinetic parameters k cat and K m . Interestingly, the natural logarithm of the bimolecular rate constant, k cat /K m , and also the natural logarithm of k cat correlate with the calculated energy of the lowest unoccupied molecular orbital of the polynitroaromatic substrates. The minimal kinetic model in line with these quantitative structure activity relationships is a ping-pong mechanism which includes substrate binding equilibria in the second half reaction.z 1999 Federation of European Biochemical Societies.

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Electron transfer reactions of Anabaena PCC 7119 ferredoxin:NADP+ reductase with nonphysiological oxidants

Cited by 35 publications

References 37 publications

Reduction of polynitroaromatic compounds: the bacterial nitroreductases

Reduction of polynitroaromatic compounds: the bacterial nitroreductases

Biotransformation of Nitro Aromatic Compounds by Flavin-Free NADHAzoreductase

Quantitative structure activity relationships for the electron transfer reactions of Anabaena PCC 7119 ferredoxin‐NADP⁺ oxidoreductase with nitrobenzene and nitrobenzimidazolone derivatives: mechanistic implications

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Electron transfer reactions of Anabaena PCC 7119 ferredoxin:NADP+ reductase with nonphysiological oxidants

Cited by 35 publications

References 37 publications

Reduction of polynitroaromatic compounds: the bacterial nitroreductases

Reduction of polynitroaromatic compounds: the bacterial nitroreductases

Biotransformation of Nitro Aromatic Compounds by Flavin-Free NADHAzoreductase

Quantitative structure activity relationships for the electron transfer reactions of Anabaena PCC 7119 ferredoxin‐NADP+ oxidoreductase with nitrobenzene and nitrobenzimidazolone derivatives: mechanistic implications

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Quantitative structure activity relationships for the electron transfer reactions of Anabaena PCC 7119 ferredoxin‐NADP⁺ oxidoreductase with nitrobenzene and nitrobenzimidazolone derivatives: mechanistic implications