2019
DOI: 10.1016/j.anaerobe.2019.03.012
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Purified thioredoxin reductase from O2-sensitive Bifidobacterium bifidum degrades H2O2 by interacting with alkyl hydroperoxide reductase

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Cited by 7 publications
(14 citation statements)
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“…A second gene encoding a thioredoxin reductase (TrxR), which has been identified in B. longum subsp. longum NCC2705 and B. bifidum JCM1255, that lacks the N-terminal domain of the disulfide reductase AhpF and seems not to be induced by O 2 stress ( 13 , 25 ) was found to be highly conserved across genomes of species included in this study ( Fig. 1 ).…”
Section: Resultsmentioning
confidence: 80%
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“…A second gene encoding a thioredoxin reductase (TrxR), which has been identified in B. longum subsp. longum NCC2705 and B. bifidum JCM1255, that lacks the N-terminal domain of the disulfide reductase AhpF and seems not to be induced by O 2 stress ( 13 , 25 ) was found to be highly conserved across genomes of species included in this study ( Fig. 1 ).…”
Section: Resultsmentioning
confidence: 80%
“…Several studies found a positive correlation between O 2 tolerance of Bifidobacterium strains and the ability to detoxify H 2 O 2 ( 20 , 69 , 70 ). Genomics and proteomics have revealed that bifidobacteria lack a gene for NADH peroxidase ( 35 , 78 ) and that an alkyl hydroperoxide reductase subunit C (AhpC) and a thioredoxin reductase-like protein (TrxR), encoded next to AhpC, instead may be responsible for H 2 O 2 decomposition ( 25 , 27 , 35 , 78 ). Our results showed that in 78% of the analyzed species, all strains harbored both an AhpC and TrxR homolog ( Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…A thioredoxin reductase-like protein (TrxR; EC 1.8.1.9; encoded by trxB) possessing the Nterminal domain of AhpF is considered to replace the function of AhpF (Fig. 4) (75,111,112). The trxB and ahpC genes are tandemly located in the genome of B. longum NCC2705 and B. bifidum ATCC 29521 (75,112).…”
Section: Molecular Mechanisms Of Oxidative Stress Responsementioning
confidence: 99%