Catalase activity at high concentration of hydrogen peroxide

Ogura, Yasuyuki

doi:10.1016/0003-9861(55)90291-5

Cited by 133 publications

(46 citation statements)

References 15 publications

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“…The K m values for hydroperoxides were too low to allow accurate determination of their values in our experiments. No other peroxide-scavenging enzyme, catalase or peroxidase, so far studied has been reported to show such high turnover numbers and low K m values for both hydrogen peroxide and alkyl hydroperoxide as described here (4,6,8,11,17,32,35,47). A recent report also describes the isolation and function of peroxiredoxin and peroxiredoxin reductase from a thermophile, Thermus aquaticus (18).…”

Section: Discussionmentioning

confidence: 61%

Hydrogen Peroxide-Forming NADH Oxidase Belonging to the Peroxiredoxin Oxidoreductase Family: Existence and Physiological Role in Bacteria

et al. 2001

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Amphibacillus xylanus and Sporolactobacillus inulinus NADH oxidases belonging to the peroxiredoxin oxidoreductase family show extremely high peroxide reductase activity for hydrogen peroxide and alkyl hydroperoxides in the presence of the small disulfide redox protein, AhpC (peroxiredoxin). In order to investigate the distribution of this enzyme system in bacteria, 15 bacterial strains were selected from typical aerobic, facultatively anaerobic, and anaerobic bacteria. AhpC-linked alkyl hydroperoxide reductase activities were detected in most of the tested strains, and especially high activities were shown in six bacterial species that grow well under aerobic conditions, including aerobic bacteria (Alcaligenes faecalis and Bacillus licheniformis) and facultatively anaerobic bacteria (Amphibacillus xylanus, Sporolactobacillus inulinus, Escherichia coli, and Salmonella enterica serovar Typhimurium). In the absence of AhpC, the purified enzymes from A. xylanus and S. inulinus catalyze the NADH-linked reduction of oxygen to hydrogen peroxide. Similar activities were observed in the cell extracts from each of these six strains. The cell extract of B. licheniformis revealed the highest AhpC-linked alkyl hydroperoxide reductase activity in the four strains, with V max values for hydrogen peroxide and alkyl hydroperoxides being similar to those for the enzymes from A. xylanus and S. inulinus. Southern blot analysis of the three strains probed with the A. xylanus peroxiredoxin reductase gene revealed single strong bands, which are presumably derived from the individual peroxiredoxin reductase genes. Single bands were also revealed in other strains which show high AhpC-linked reductase activities, suggesting that the NADH oxidases belonging to the peroxiredoxin oxidoreductase family are widely distributed and possibly play an important role both in the peroxide-scavenging systems and in an effective regeneration system for NAD in aerobically growing bacteria.NADH oxidases are found in several microorganisms (9,12,20,31,41) and have been purified from at least nine bacterial species (7,10,13,25,30,34,40,42,44). There are two types of NADH oxidase, H 2 O forming and hydrogen peroxide forming. We previously purified the hydrogen peroxide-forming NADH oxidases from aerobically grown Amphibacillus xylanus and Sporolactobacillus inulinus, both of which are facultatively anaerobic bacteria that lack a respiratory chain (25, 30). The physiological function of these enzymes was first thought to be the in vivo regeneration of NAD in aerobic metabolism of the bacteria (22-24, 30). The enzymes catalyze the reduction of oxygen by NADH to form hydrogen peroxide. However, in the presence of a 21-kDa disulfide-containing redox protein (AhpC), now commonly referred to as peroxiredoxin (Prx), the NADH oxidases also showed extremely high reductase activity for both hydrogen peroxide and alkyl hydroperoxides (26,(28)(29)(30). These NADH oxidases thus belong to a growing new family of peroxiredoxin oxidoreductases (PrxR) (38) and are involved...

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Section: Discussionmentioning

confidence: 61%

Hydrogen Peroxide-Forming NADH Oxidase Belonging to the Peroxiredoxin Oxidoreductase Family: Existence and Physiological Role in Bacteria

et al. 2001

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“…This is severalfold lower than the value (4.3 ϫ 10 5 M Ϫ1 s Ϫ1 ) obtained with CuOOH and lipoamide as reductant (Table 3) but likely represents a lower limit, since the substrate concentrations were not fully optimized. These rates are two orders of magnitude lower than the value (4 ϫ 10 7 M Ϫ1 s Ϫ1 ) for catalase with H 2 O 2 that is considered to be close to diffusion controlled (18,47).…”

Section: Resultsmentioning

confidence: 67%

Organic Hydroperoxide Resistance Protein and Ergothioneine Compensate for Loss of Mycothiol in Mycobacterium smegmatis Mutants

Buchmeier

Newton

et al. 2011

J Bacteriol

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The mshA::Tn5 mutant of Mycobacterium smegmatis does not produce mycothiol (MSH) and was found to markedly overproduce both ergothioneine and an ϳ15-kDa protein determined to be organic hydroperoxide resistance protein (Ohr). An mshA(G32D) mutant lacking MSH overproduced ergothioneine but not Ohr. Comparison of the mutant phenotypes with those of the wild-type strain indicated the following: Ohr protects against organic hydroperoxide toxicity, whereas ergothioneine does not; an additional MSH-dependent organic hydroperoxide peroxidase exists; and elevated isoniazid resistance in the mutant is associated with both Ohr and the absence of MSH. Purified Ohr showed high activity with linoleic acid hydroperoxide, indicating lipid hydroperoxides as the likely physiologic targets. The reduction of oxidized Ohr by NADH was shown to be catalyzed by lipoamide dehydrogenase and either lipoamide or DlaT (SucB). Since free lipoamide and lipoic acid levels were shown to be undetectable in M. smegmatis, the bound lipoyl residues of DlaT are the likely source of the physiological dithiol reductant for Ohr. The pattern of occurrence of homologs of Ohr among bacteria suggests that the ohr gene has been distributed by lateral transfer. The finding of multiple Ohr homologs with various sequence identities in some bacterial genomes indicates that there may be multiple physiologic targets for Ohr proteins. Mycobacteria, including Mycobacterium tuberculosis, produce mycothiol (MSH) as the major intracellular thiol (39).Like glutathione in eukaryotes and Gram-negative bacteria, MSH has a wide range of functions that include detoxification of electrophilic compounds, conjugation with antibiotics, and maintenance of the redox potential within the cell (30,42,53). The biosynthesis of mycothiol requires five enzymes (Fig. 1), MshA, MshA2, MshB, MshC, and MshD (44). Mutants with mutations of mshA and mshC produce undetectable levels of mycothiol, whereas mshB and mshD mutants make ϳ10% and 1% of normal levels, respectively, during exponential growth (42). The mshD mutant also produces high levels of the precursor to mycothiol and two related thiols in which the acetyl residue of mycothiol is replaced by formyl or succinyl residues. The decreased levels of mycothiol in mshB and mshD mutants are thought to involve alternative low-level pathways, whereas MshA, a glycosyltransferase, and MshC, a homolog of cysteine tRNA synthetase, do not have compensating enzymes. Several of the mycothiol mutants of Mycobacterium smegmatis have been characterized and exhibit increased sensitivity to peroxides, alkylating agents, and antibiotics (53).Mycothiol has been of special interest due to its apparent requirement for the growth of M. tuberculosis (5, 58). Like the M. smegmatis mutants, M. tuberculosis mutants bearing mutations of the mshB (7) and mshD (6) genes have decreased levels of mycothiol and increased sensitivity to peroxides. Attempts to generate viable mutants with mutations of the native mshA (5) and mshC (58) genes in M. tuberculosis were unsu...

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“…K m values for hydrogen peroxide, cumene hydroperoxide, and NADH are too low to allow accurate determination of their values in these experiments. Several enzymes that show scavenging activity for hydrogen peroxide and alkyl hydroperoxides have been purified and characterized from bacteria or mammalian sources (9,11,(21)(22)(23)(24)(25)(26). The V max value for the flavin-containing NADH peroxidase from Streptococcus faecalis is 121 s Ϫ1 at pH 5.4 (9).…”

Section: Discussionmentioning

confidence: 99%

“…In evaluating the stoichiometries of NADH reduction on addition of a limiting amount of hydrogen peroxide in anaerobic turnover experiments, standardization of the hydrogen peroxide was carried out by addition of 6 -10 l of a stock hydrogen peroxide solution (88 mM) to a 1-ml reaction mixture containing 0.01% o-dianisidine and 20 g of horseradish peroxidase (12). The stoichiometry of the NADH oxidase reaction was determined aerobically under conditions of limiting NADH (21,41, and 62 nmol), and the amount of hydrogen peroxide produced was assayed using the o-dianisidine/horseradish peroxidase system (12).…”

Section: Methodsmentioning

confidence: 99%

Amphibacillus xylanus NADH Oxidase and Salmonella typhimurium Alkyl-hydroperoxide Reductase Flavoprotein Components Show Extremely High Scavenging Activity for Both Alkyl Hydroperoxide and Hydrogen Peroxide in the Presence of S. typhimurium Alkyl-hydroperoxide Reductase 22-kDa Protein Component

Niimura

Poole

Massey

1995

Journal of Biological Chemistry

106

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The flavoprotein NADH oxidase from Amphibacillus xylanus consumes oxygen to produce hydrogen peroxide. The amino acid sequence of this flavoprotein shows 51.2% identity to the F-52a component, denoted AhpF, of the alkyl-hydroperoxide reductase from Salmonella typhimurium. AhpF also catalyzes NADH-dependent hydrogen peroxide formation under aerobic conditions, albeit at a somewhat slower rate than the Amphibacillus protein. In the presence of the 22-kDa colorless component (AhpC) of the Salmonella alkyl-hydroperoxide reductase, both proteins catalyze the 4-electron reduction of oxygen to water. Both flavoproteins are active as AhpC reductases and mediate electron transfer, resulting in the NADH-dependent reduction of hydrogen peroxide and cumene hydroperoxide. Both enzymes' K m values for hydrogen peroxide, cumene hydroperoxide, and NADH are so low that they could not be determined accurately. V max values for hydrogen peroxide or cumene hydroperoxide reduction are >10,000 min ؊1 at 25°C. These values are almost the same as the reduction rate of the flavoprotein component by NADH. The involvement in catalysis of a redox-active disulfide of the A. xylanus flavoprotein was shown by construction of three mutant enzymes, C337S, C340S, and C337S/C340S. Very little activity for hydrogen peroxide or cumene hydroperoxide was found with the single mutants (C337S and C340S), and none with the double mutant (C337S/C340S).Analysis of the DNA sequence upstream of the Amphibacillus flavoprotein structural gene indicated the presence of a partial open reading frame homologous to the Salmonella ahpC structural gene (64.3% identical at the amino acid sequence level), suggesting that the NADH oxidase protein of A. xylanus is also part of a functional alkyl-hydroperoxide reductase system within these catalase-lacking bacteria.We recently have isolated a new group of facultatively anaerobic bacteria from alkaline compost (1). The bacteria have unique phenotypic and chemotaxonomic characteristics (2) as well as bioenergetic properties (3) and were named Amphibacillus xylanus (2). A. xylanus, lacking a respiratory system and hemeproteins, catalase, and peroxidase, grows well and has the same growth rate and cell yield under strictly anaerobic and aerobic conditions (2). This growth characteristic of A. xylanus is due to the presence of anaerobic and aerobic pathways producing similar amounts of ATP (4). Under aerobic conditions, NADH is thought to be responsible for maintenance of the intracellular redox balance (4).A flavoprotein functional as NADH oxidase was purified from aerobically grown A. xylanus (5). The flavoprotein is a homotetramer composed of subunits (M r ϭ 56,000) containing 1 mol of FAD and also catalyzes a thiol-disulfide interchange reaction, NADH:DTNB 1 oxidoreductase (6). The complete reduction of enzyme by dithionite requires 6 electrons/subunit (6). Such behavior indicates the presence of redox centers in addition to the FAD, and these were postulated to be disulfides (6). To assess the catalytic role of disulfide...

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Catalase activity at high concentration of hydrogen peroxide

Cited by 133 publications

References 15 publications

Hydrogen Peroxide-Forming NADH Oxidase Belonging to the Peroxiredoxin Oxidoreductase Family: Existence and Physiological Role in Bacteria

Hydrogen Peroxide-Forming NADH Oxidase Belonging to the Peroxiredoxin Oxidoreductase Family: Existence and Physiological Role in Bacteria

Organic Hydroperoxide Resistance Protein and Ergothioneine Compensate for Loss of Mycothiol in Mycobacterium smegmatis Mutants

Amphibacillus xylanus NADH Oxidase and Salmonella typhimurium Alkyl-hydroperoxide Reductase Flavoprotein Components Show Extremely High Scavenging Activity for Both Alkyl Hydroperoxide and Hydrogen Peroxide in the Presence of S. typhimurium Alkyl-hydroperoxide Reductase 22-kDa Protein Component

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