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Direct synthesis of hydrogen peroxide from hydrogen and oxygen by using a water-soluble iridium complex and flavin mononucleotide.

ABSTRACT: H2 , O2 to H2 O2 : The direct synthesis of hydrogen peroxide from hydrogen and oxygen in water has been made possible by using an iridium(III) complex, [Ir(III) (Cp*)(4-(1H-pyrazol-1-yl-κN(2) )benzoic acid-κC(3) )(H2 O)]2 SO4 , and flavin mononucleotide. This method gives hydrogen peroxide with a high turnover number (847) and yield (19.2 %) under normal pressure and at room temperature.

SUBMITTER: Shibata S

PROVIDER: S-EPMC4138997 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature

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Direct synthesis of hydrogen peroxide from hydrogen and oxygen by using a water-soluble iridium complex and flavin mononucleotide.

Shibata Satoshi S Suenobu Tomoyoshi T Fukuzumi Shunichi S

Angewandte Chemie (International ed. in English) 20131025 47

H2 , O2 to H2 O2 : The direct synthesis of hydrogen peroxide from hydrogen and oxygen in water has been made possible by using an iridium(III) complex, [Ir(III) (Cp*)(4-(1H-pyrazol-1-yl-κN(2) )benzoic acid-κC(3) )(H2 O)]2 SO4 , and flavin mononucleotide. This method gives hydrogen peroxide with a high turnover number (847) and yield (19.2 %) under normal pressure and at room temperature. ...[more]

PMID: 24166980

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Project description:Soil bacteria can detoxify Cr(VI) ions by reduction. Within the last 2 decades, numerous reports of chromate reductase enzymes have been published. These reports describe catalytic reduction of chromate ions by specific enzymes. These enzymes each have sequence similarity to known redox-active flavoproteins. We investigated the enzyme NfoR from Staphylococcus aureus, which was reported to be upregulated in chromate-rich soils and to have chromate reductase activity (H. Han, Z. Ling, T. Zhou, R. Xu, et al., Sci Rep 7:15481, 2017, https://doi.org/10.1038/s41598-017-15588-y). We show that NfoR has structural similarity to known flavin mononucleotide (FMN) reductases and reduces FMN as a substrate. NfoR binds FMN with a dissociation constant of 0.4 μM. The enzyme then binds NADPH with a dissociation constant of 140 μM and reduces the flavin at a rate of 1,350 s-1 Turnover of the enzyme is apparently limited by the rate of product release that occurs, with a net rate constant of 0.45 s-1 The rate of product release limits the rate of observed chromate reduction, so the net rate of chromate reduction by NfoR is orders of magnitude lower than when this process occurs in solution. We propose that NfoR is an FMN reductase and that the criterion required to define chromate reduction as enzymatic has not been met. That NfoR expression is increased in the presence of chromate suggests that the survival adaption was to increase the net rate of chromate reduction by facile, adventitious redox processes.IMPORTANCE Chromate is a toxic by-product of multiple industrial processes. Chromate reduction is an important biological activity that ameliorates Cr(VI) toxicity. Numerous researchers have identified chromate reductase activity by observing chromate reduction. However, all identified chromate reductase enzymes have flavin as a cofactor or use a flavin as a substrate. We show here that NfoR, an enzyme claimed to be a chromate reductase, is in fact an FMN reductase. In addition, we show that reduction of a flavin is a viable way to transfer electrons to chromate but that it is unlikely to be the native function of enzymes. We propose that upregulation of a redox-active flavoprotein is a viable means to detoxify chromate that relies on adventitious reduction that is not catalyzed.

Dataset Information

Direct synthesis of hydrogen peroxide from hydrogen and oxygen by using a water-soluble iridium complex and flavin mononucleotide.

Publications

Direct synthesis of hydrogen peroxide from hydrogen and oxygen by using a water-soluble iridium complex and flavin mononucleotide.

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