Crystalline bacterial catalase

Herbert, D.; Pinsent, Jane

doi:10.1042/bj0430193

Cited by 138 publications

(25 citation statements)

References 17 publications

(11 reference statements)

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“…Monofunctional catalases are the earliest known bacterial catalases [40, 41] and are virtually ubiquitous among both aerobic and anaerobic bacteria. Bifunctional catalases are less abundant; as of November 2011, 435 catalase-peroxidase sequences were deposited in the peroxibase data set [42].…”

Section: Why So Many Scavengers Of H2o2? General Considerationsmentioning

confidence: 99%

Why do bacteria use so many enzymes to scavenge hydrogen peroxide?

Mishra

Imlay

2012

Archives of Biochemistry and Biophysics

343

301

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Hydrogen peroxide (H2O2) is continuously formed by the autoxidation of redox enzymes in aerobic cells, and it also enters from the environment, where it can be generated both by chemical processes and by the deliberate actions of competing organisms. Because H2O2 is acutely toxic, bacteria elaborate scavenging enzymes to keep its intracellular concentration at nanomolar levels. Mutants that lack such enzymes grow poorly, suffer from high rates of mutagenesis, or even die. In order to understand how bacteria cope with oxidative stress, it is important to identify the key enzymes involved in H2O2 degradation. Catalases and NADH peroxidase (Ahp) are primary scavengers in many bacteria, and their activities and physiological impacts have been unambiguously demonstrated through phenotypic analysis and through direct measurements of H2O2 clearance in vivo. Yet a wide variety of additional enzymes have been proposed to serve similar roles: thiol peroxidase, bacterioferritin comigratory protein, glutathione peroxidase, cytochrome c peroxidase, and rubrerythrins. Each of these enzymes can degrade H2O2 in vitro, but their contributions in vivo remain unclear. In this review we examine the genetic, genomic, regulatory, and biochemical evidence that each of these is a bona fide scavenger of H2O2 in the cell. We also consider possible reasons that bacteria might require multiple enzymes to catalyze this process, including differences in substrate specificity, compartmentalization, cofactor requirements, kinetic optima, and enzyme stability. It is hoped that the resolution of these issues will lead to an understanding of stress resistance that is more accurate and perceptive.

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Section: Why So Many Scavengers Of H2o2? General Considerationsmentioning

confidence: 99%

Why do bacteria use so many enzymes to scavenge hydrogen peroxide?

Mishra

Imlay

2012

Archives of Biochemistry and Biophysics

343

301

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“…of the soluble protein would appear reasonable. It is certainly far lower than the catalase content of Micrococcus lysodeicticus found by Herbert and Pinsent (1948); this was 1-2 per cent. of the dry weight, or of the order of 2-4 per cent.…”

Section: (D) Reconstruction Of Concentrated Systems Without Carriersmentioning

confidence: 67%

Bacterial Oxidation of Arsenite IV. Some Properties of the Bacterial Cytochromes

Legge¹

1954

Aust. Jnl. Of Bio. Sci.

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SummaryCytochromes band c were observed in all subs trains of Pseudomonas arsenoxydans-quinque examined; in some substrains, however, cytochrome a was not visible. Such strains poor in cytochrome a were less efficient arsenite oxidizers than those in which this cytochrome component was detectable.The cytochromes were associated with the insoluble fraction obtained after grinding the packed cells with powdered glass, only traces of cytochrome c being found in the soluble fraction.A significant rate of arsenite oxidation in systems reconstructed from dehydrogenase and oxidase was observed either when both fractions were present in relatively high concentration (about one-seventh that within the cell) or when an artificial carrier (2,6-dichlorophenol indophenol) was present.Mammalian cytochrome c proved ineffective as a carrier. No evidence could be obtained that any natural carrier was present, and calculations indicate that diffusion of the arsenite dehydrogenase-arsenite complex could account for the oxygen uptake found in intact cells without any more readily diffusible electron carrier.

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“…The very high concentration (1 to 2 per cent) of catalase in M. lysodeikti cus (93) indicates that the biological function of catalase is not simply the destruction of hydrogen peroxide, thereby strengthening the suggestion put forward by Keilin & Hartree (113) that some other function, probably peroxidative, must be sought for the enzyme. According to Chance (103),…”

Section: Bile Pigments and Dipyrrolic Substancesmentioning

confidence: 72%