scholarly journals Organoiridium–quinone conjugates for facile hydrogen peroxide generation

2020 ◽  
Vol 56 (87) ◽  
pp. 13381-13384
Author(s):  
Huong T. H. Nguyen ◽  
Loi H. Do

Tethered iridium–quinone catalyst in the presence of air and sodium formate generates H2O2 more rapidly than iridium and quinone mixtures at low catalyst concentration.

ACS Catalysis ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 2454-2459
Author(s):  
Zhe Wang ◽  
Qin-Kun Li ◽  
Chenhao Zhang ◽  
Zhihua Cheng ◽  
Weiyin Chen ◽  
...  

Redox Biology ◽  
2021 ◽  
Vol 43 ◽  
pp. 101980
Author(s):  
Andree G. Pearson ◽  
Juliet M. Pullar ◽  
John Cook ◽  
Emma S. Spencer ◽  
Margreet CM. Vissers ◽  
...  

2003 ◽  
Vol 279 (3) ◽  
pp. 1665-1675 ◽  
Author(s):  
Juan A. Rosado ◽  
Pedro C. Redondo ◽  
Ginés M. Salido ◽  
Emilio Gómez-Arteta ◽  
Stewart O. Sage ◽  
...  

1991 ◽  
Vol 18 (2) ◽  
pp. 133-143 ◽  
Author(s):  
Hiroshi Ogasawara ◽  
Shiro Yoshimura ◽  
Takeo Kumoi

2019 ◽  
Vol 74 (3-4) ◽  
pp. 101-104 ◽  
Author(s):  
Milja Pesic ◽  
Sébastien Jean-Paul Willot ◽  
Elena Fernández-Fueyo ◽  
Florian Tieves ◽  
Miguel Alcalde ◽  
...  

Abstract There is an increasing interest in the application of peroxygenases in biocatalysis, because of their ability to catalyse the oxyfunctionalisation reaction in a stereoselective fashion and with high catalytic efficiencies, while using hydrogen peroxide or organic peroxides as oxidant. However, enzymes belonging to this class exhibit a very low stability in the presence of peroxides. With the aim of bypassing this fast and irreversible inactivation, we study the use of a gradual supply of hydrogen peroxide to maintain its concentration at stoichiometric levels. In this contribution, we report a multienzymatic cascade for in situ generation of hydrogen peroxide. In the first step, in the presence of NAD+ cofactor, formate dehydrogenase from Candida boidinii (FDH) catalysed the oxidation of formate yielding CO2. Reduced NADH was reoxidised by the reduction of the flavin mononucleotide cofactor bound to an old yellow enzyme homologue from Bacillus subtilis (YqjM), which subsequently reacts with molecular oxygen yielding hydrogen peroxide. Finally, this system was coupled to the hydroxylation of ethylbenzene reaction catalysed by an evolved peroxygenase from Agrocybe aegerita (rAaeUPO). Additionally, we studied the influence of different reaction parameters on the performance of the cascade with the aim of improving the turnover of the hydroxylation reaction.


1987 ◽  
Vol 253 (4) ◽  
pp. C495-C499 ◽  
Author(s):  
P. D. Walker ◽  
S. V. Shah

Agents that affect mitochondrial respiration have been shown to enhance the generation of reactive oxygen metabolites. On the basis of the well-demonstrated ability of gentamicin to alter mitochondrial respiration (stimulation of state 4 and inhibition of state 3), it was postulated that gentamicin may enhance the generation of reactive oxygen metabolites by renal cortical mitochondria. The aim of this study was to examine the effect of gentamicin on the production of hydrogen peroxide (measured as the decrease in scopoletin fluorescence) in rat renal cortical mitochondria. The hydrogen peroxide generation by mitochondria was enhanced from 0.17 +/- 0.02 nmol . mg-1 . min-1 (n = 14) in the absence of gentamicin to 6.21 +/- 0.67 nmol . mg-1 . min-1 (n = 14) in the presence of 4 mM gentamicin. This response was dose dependent with a significant increase observed at even the lowest concentration of gentamicin tested, 0.01 mM. Production of hydrogen peroxide was not increased when gentamicin was added to incubation media in which mitochondria or substrate was omitted or heat-inactivated mitochondria were used. The gentamicin-induced change in fluorescence was completely inhibited by catalase (but not by heat-inactivated catalase), indicating that the decrease in fluorescence was due to hydrogen peroxide. Thus this study demonstrates that gentamicin enhances the production of hydrogen peroxide by mitochondria. Because of their well-documented cytotoxicity, reactive oxygen metabolites may play a critical role in gentamicin nephrotoxicity.


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