Hydroxylation of aromatic compounds by reduced nicotinamide-adenine dinucleotide and phenazine methosulphate requires hydrogen peroxide and hydroxyl radicals, but not superoxide

Halliwell, Barry

doi:10.1042/bj1670317

Cited by 27 publications

(3 citation statements)

References 15 publications

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“…The reaction of NADH with PMS to give the fully reduced form of PMS (5,10-dihydro-5-methylphenazine) and the interaction of reduced PMS with oxygen has been examined in several laboratories (Nishikimi et al, 1972;Halaka et al, 1982;; these studies have suggested that superoxide radical (02~•) or hydroxyl radical (HO•) is formed from oxygen and reduced PMS. In fact, the NADH/PMS/02 system has been shown to be capable of hydroxylating aromatic substrates (Prema Kumar, 1972;Halliwell, 1977). The possibility that these types of nonenzymatically formed activated oxygen species are involved in the PMS-mediated hydroxylation of camphor reported here is eliminated by the control experiments.…”

Section: Discussionmentioning

confidence: 65%

NADH- and oxygen-dependent multiple turnovers of cytochrome P-450-CAM without putidaredoxin and putidaredoxin reductase

Eble¹,

Dawson²

1984

Biochemistry

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Phenazine methosulfate (PMS) has been successfully used to mediate electron transfer from NADH to cytochrome P-450-CAM in the absence of putidaredoxin and putidaredoxin reductase under aerobic conditions. Identification and quantitation of exo-5- hydroxycamphor , the only product, has been accomplished by gas chromatography. In the absence of cytochrome P-450-CAM, or when other heme proteins (hemoglobin, myoglobin, horseradish peroxidase) are substituted for P-450-CAM, no exo-5- hydroxycamphor is detected. Product formation is not inhibited by the addition of catalase, superoxide dismutase, or hydroxyl radical scavengers; however, significant inhibition is observed with carbon monoxide and metyrapone, known inhibitors of the fully reconstituted P-450 system. Addition of 2,3-dimercaptopropanol to the NADH/PMS/P-450 system leads to a 4-fold increase in product formation; when putidaredoxin is added (without dimercaptopropanol), a 20-fold increase in product formation is observed. Constant bubbling with oxygen results in a further increase in the amount of product (150-fold increase overall). Our results show that PMS can substitute for the electron-transfer proteins putidaredoxin and putidaredoxin reductase in the transfer of electrons from NADH to P-450-CAM, resulting in multiple turnovers. Molecular oxygen dependent multiple turnovers of cytochrome P-450 have not been previously observed without the fully reconstituted, three-protein system.

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Section: Discussionmentioning

confidence: 65%

NADH- and oxygen-dependent multiple turnovers of cytochrome P-450-CAM without putidaredoxin and putidaredoxin reductase

Eble¹,

Dawson²

1984

Biochemistry

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“…If enzymatic reactions, for instance by intracellular oxidoreductases, were the main mechanism for redox cycling, AGA and GA would have the same effec- tive redox activity in the intracellular environment. However, with NADPH and NADH able to reduce the phenazines directly, albeit at a slower rate [18,19] it may well be that the reduced pyridine nucleotides are sufficiently abundant for direct reduction to predominate. This would account for the much greater cytotoxic effect of AGA since it is more readily reduced by such nucleotides than GA.…”

Section: Aga Activitymentioning

confidence: 97%

Investigations into the in vitro antimicrobial activity and mode of action of the phenazine antibiotic d-alanylgriseoluteic acid

Giddens

Bean

2007

International Journal of Antimicrobial Agents

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“…The reaction of PMS and NADH has been reported to produce hydrogen peroxide, 47 which at high enough levels may contribute to enzyme activity. To test this possibility, 1 μM catalase was included in the CmlI/pAP/NADH/PMS reaction.…”

Section: ■ Introductionmentioning

confidence: 99%

Enhanced Arylamine N-Oxygenase Activity of Polymer–Enzyme Assemblies by Facilitating Electron-Transferring Efficiency

Zhang

Makris

et al. 2018

Biomacromolecules

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A novel N-oxygenase-coated core-shell nanoparticle was generated through the coassembly of poly(4-vinylpyridine) (P4VP) and arylamine N-oxygenase CmlI. The resulting enzyme-hybridized particles, P4VP-CmlI, showed excellent catalytic activities on the oxidation of two arylamine substrates, i.e., p-aminophenol ( pAP) and p-aminobenzoic acid ( pABA), using a surrogate redox system or a peroxide shunt as co-oxidants. In comparison with the free enzyme, P4VP-CmlI particles exhibited a significantly enhanced catalytic efficiency when using pyridine nucleotide (NADH) and proper redox mediators. Products at different oxygenation stages were observed. On the contrary, the activity of the enzyme-containing nanoparticles was very similar to the free enzyme when using the peroxide shunt. The enhanced catalytic efficiency of the P4VP-CmlI assemblies is attributed to a more efficient electron delivery.

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Hydroxylation of aromatic compounds by reduced nicotinamide-adenine dinucleotide and phenazine methosulphate requires hydrogen peroxide and hydroxyl radicals, but not superoxide

Cited by 27 publications

References 15 publications

NADH- and oxygen-dependent multiple turnovers of cytochrome P-450-CAM without putidaredoxin and putidaredoxin reductase

NADH- and oxygen-dependent multiple turnovers of cytochrome P-450-CAM without putidaredoxin and putidaredoxin reductase

Investigations into the in vitro antimicrobial activity and mode of action of the phenazine antibiotic d-alanylgriseoluteic acid

Enhanced Arylamine N-Oxygenase Activity of Polymer–Enzyme Assemblies by Facilitating Electron-Transferring Efficiency

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