ArticleJournal of bacteriology2004
KatG is the primary detoxifier of hydrogen peroxide produced by aerobic metabolism in Bradyrhizobium japonicum.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 60 citations in OpenAlex.
- Manipulating Intracellular Oxidative Conditions to Enhance Porphyrin Production inBioengineering (Basel, Switzerland) · 2025Article
- Catalase-peroxidase (KatG): a potential frontier in tuberculosis drug development.Critical reviews in biochemistry and molecular biology · 2024Review
- The divalent metal ion exporter IhpABC is required to maintain iron homeostasis under low to moderate environmental iron conditions in the bacterium Bradyrhizobium japonicum.Molecular microbiology · 2024Article
- Cytosol Peroxiredoxin and Cell Surface Catalase Differentially Respond to HAntioxidants (Basel, Switzerland) · 2023Article
- Critical Effect of HMicrobiology spectrum · 2022Article
- Mechanisms underlying interactions between two abundant oral commensal bacteria.The ISME journal · 2022Article
- Redox Regulation in Diazotrophic Bacteria in Interaction with Plants.Antioxidants (Basel, Switzerland) · 2021Review
- Quantitative proteomic analysis of ahpC/F and katE and katG knockout Escherichia coli-a useful model to study endogenous oxidative stress.Applied microbiology and biotechnology · 2021Article
- Catalase Expression in Azospirillum brasilense Sp7 Is Regulated by a Network Consisting of OxyR and Two RpoH Paralogs and Including an RpoE1→RpoH5 Regulatory Cascade.Applied and environmental microbiology · 2018Article
- Rapid evolution of a bacterial iron acquisition system.Molecular microbiology · 2018Article
- Involvement of multiple stressors induced by non-thermal plasma-charged aerosols during inactivation of airborne bacteria.PloS one · 2017Article
- Ozone Sensitivity and Catalase Activity in Pigmented and Non-Pigmented Strains ofThe open microbiology journal · 2017Article
- Metal-specific control of gene expression mediated by Bradyrhizobium japonicum Mur and Escherichia coli Fur is determined by the cellular context.Molecular microbiology · 2016Article
- Hfq plays important roles in virulence and stress adaptation in Cronobacter sakazakii ATCC 29544.Infection and immunity · 2015Article
- Magnesium-dependent processes are targets of bacterial manganese toxicity.Molecular microbiology · 2014Article
- Manganese is required for oxidative metabolism in unstressed Bradyrhizobium japonicum cells.Molecular microbiology · 2012Article
- Article
- Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis.Antioxidants & redox signaling · 2011Review
- Genome-wide transcriptional and physiological responses of Bradyrhizobium japonicum to paraquat-mediated oxidative stress.Applied and environmental microbiology · 2011Article
- Regulation of catalase-peroxidase KatG is OxyR dependent and Fur independent in Caulobacter crescentus.Journal of bacteriology · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Bacteria are exposed to reactive oxygen species from the environment and from those generated by aerobic metabolism. Catalases are heme proteins that detoxify H(2)O(2), and many bacteria contain more than one catalase enzyme. Also, the nonheme peroxidase alkyl hydroperoxide reductase (Ahp) is the major scavenger of endogenous H(2)O(2) in Escherichia coli. Here, we show that aerobically grown Bradyrhizobium japonicum cells express a single catalase activity. Four genes encoding putative catalases in the B. japonicum genome were identified, including a katG homolog encoding a catalase-peroxidase. Deletion of the katG gene resulted in loss of catalase activity in cell extracts and of exogenous H(2)O(2) consumption by whole cells. The katG strain had a severe aerobic growth phenotype but showed improved growth in the absence of O(2). By contrast, a B. japonicum ahpCD mutant grew well aerobically and consumed H(2)O(2) at wild-type rates. A heme-deficient hemA mutant expressed about one-third of the KatG activity as the wild type but grew well aerobically and scavenged low concentrations of exogenous H(2)O(2). However, cells of the hemA strain were deficient in consumption of high concentrations of H(2)O(2) and were very sensitive to killing by short exposure to H(2)O(2). In addition, KatG activity did not decrease as a result of mutation of the gene encoding the transcriptional activator OxyR. We conclude that aerobic metabolism produces toxic levels of H(2)O(2) in B. japonicum, which is detoxified primarily by KatG. Furthermore, the katG level sufficient for detoxification does not require OxyR.
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