Common phylogeny of catalase-peroxidases and ascorbate peroxidases

Zámocký, Marcel; Janeček, Štefan; Koller, Franz

doi:10.1016/s0378-1119(00)00358-9

Cited by 50 publications

(44 citation statements)

References 24 publications

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“…An N. gonorrhoeae ccp mutant strain showed slight sensitivity to in vitro hydrogen peroxide killing relative to the wild-type strain; however, a ccp/katA double mutant strain was significantly more sensitive to in vitro hydrogen peroxide killing than was a katA mutant strain (213,239). Ccp belongs to class I of the peroxidase superfamily, along with catalase-peroxidases and ascorbate peroxidases (260). It is a diheme c-type cytochrome that catalyzes the reduction of hydrogen peroxide using c-type cytochromes of the respiratory chain as the electron donor (reaction 7):…”

Section: Peroxidase: Cytochrome C Peroxidasementioning

confidence: 99%

Defenses against Oxidative Stress inNeisseria gonorrhoeae: a System Tailored for a Challenging Environment

Seib

Kidd

et al. 2006

Microbiol Mol Biol Rev

129

174

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SUMMARY Neisseria gonorrhoeae is a host-adapted pathogen that colonizes primarily the human genitourinary tract. This bacterium encounters reactive oxygen and reactive nitrogen species as a consequence of localized inflammatory responses in the urethra of males and endocervix of females and also of the activity of commensal lactobacilli in the vaginal flora. This review describes recent advances in the understanding of defense systems against oxidative stress in N. gonorrhoeae and shows that while some of its defenses have similarities to the paradigm established with Escherichia coli, there are also some key differences. These differences include the presence of a defense system against superoxide based on manganese ions and a glutathione-dependent system for defense against nitric oxide which is under the control of a novel MerR-like transcriptional regulator. An understanding of the defenses against oxidative stress in N. gonorrhoeae and their regulation may provide new insights into the ways in which this bacterium survives challenges from polymorphonuclear leukocytes and urogenital epithelial cells.

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Section: Peroxidase: Cytochrome C Peroxidasementioning

confidence: 99%

Defenses against Oxidative Stress inNeisseria gonorrhoeae: a System Tailored for a Challenging Environment

Seib

Kidd

et al. 2006

Microbiol Mol Biol Rev

129

174

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“…Catalase, an enzyme found in both prokaryotes and eukaryotes, detoxifies H 2 O 2 into water and oxygen (Zamocky & Koller, 1999), and it can be grouped into three distinct enzyme families: mono-functional catalases (HPII class), bifunctional catalase/peroxidases (HPI class), and manganese-dependent catalases (Switala & Loewen, 2002;Zamocky & Koller, 1999;Zamocky et al, 2000). Bifunctional catalase/peroxidases are haem co-factored enzymes that have been described in simple eukaryotes and prokaryotes, and are evolutionarily linked to plant peroxidases (Zamocky & Koller, 1999;Zamocky et al, 2000). This class of enzymes has been associated with virulence in various bacterial pathogens, including Legionella pneumophila and Agrobacterium tumefaciens (Bandyopadhyay & Steinman, 1998Bandyopadhyay et al, 2003;Xu & Pan, 2000).…”

Section: Introductionmentioning

confidence: 99%

A minor catalase/peroxidase from Burkholderia cenocepacia is required for normal aconitase activity

2005

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The opportunistic bacterium Burkholderia cenocepacia C5424 contains two catalase/peroxidase genes, katA and katB. To investigate the functions of these genes, katA and katB mutants were generated by targeted integration of suicide plasmids into the katA and katB genes. The catalase/peroxidase activity of the katA mutant was not affected as compared with that of the parental strain, while no catalase/peroxidase activity was detected in the katB mutant. However, the katA mutant displayed reduced resistance to hydrogen peroxide under iron limitation, while the katB mutant showed hypersensitivity to hydrogen peroxide, and reduced growth under all conditions tested. The katA mutant displayed reduced growth only in the presence of carbon sources that are metabolized through the tricarboxylic acid (TCA) cycle, as the growth defect was abrogated in cultures supplemented with glucose or glycerol. This phenotype was also correlated with a marked reduction in aconitase activity. In contrast, aconitase activity was not reduced in the katB mutant and parental strains. The authors conclude that the KatA protein is a specialized catalase/peroxidase that has a novel function by contributing to maintain the normal activity of the TCA cycle, while KatB is a classical catalase/peroxidase that plays a global role in cellular protection against oxidative stress.

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“…Bacterial cytochrome c peroxidases (CcP) are periplasmic enzymes found in bacteria, which carry out the 2-electron reduction of hydrogen peroxide (4). The characterized examples of bacterial peroxidases are all diheme enzymes, making them distinct from the superfamily of plant and yeast peroxidases that contain a single heme unit (5,6). It has been proposed that the bacterial diheme enzymes store electron equivalents differently than the monoheme-type CcPs; while the latter are known to generate Compound I in the course of catalysis (containing either a porphyrin radical or an oxidized Trp residue) (7), the bacterial enzymes appear to use a ferrous secondary heme of high potential (H) to store the same electron equivalent needed to generate the radical-based Compound I in monoheme CcPs (8).…”

mentioning

confidence: 99%

A Distinctive Electrocatalytic Response from the Cytochrome c Peroxidase of Nitrosomonas europaea

Bradley

Chobot

Arciero

et al. 2004

Journal of Biological Chemistry

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Here the cytochrome c peroxidase (CcP) from Nitrosomonas europaea is examined using the technique of catalytic protein film voltammetry. Submonolayers of the bacterial diheme enzyme at a pyrolytic graphite edge electrode give catalytic, reductive signals in the presence of the substrate hydrogen peroxide. The resulting waveshapes indicate that CcP is bound non-covalently in a highly active configuration. The native enzyme has been shown to possess two heme groups of low and high potential (L and H, ؊260 and ؉450 mV versus hydrogen, respectively), and here we find that the catalytic waves of the N. europaea enzyme have a midpoint potential of >500 mV and a shape that corresponds to a 1-electron process. The signals increase in magnitude with hydrogen peroxide concentration, revealing Michaelis-Menten kinetics and K m ‫؍‬ 55 M. The midpoint potentials shift with substrate concentration, indicating the electrochemically active species observed in our data corresponds to a catalytic species. The potentials also shift with respect to pH, and the pH dependence is interpreted in terms of a two pK a model for proton binding. Together the data show that the electrochemistry of the N. europaea cytochrome c peroxidase is unlike other peroxidases studied to date, including other bacterial enzymes. This is discussed in terms of a catalytic model for the N. europaea enzyme and compared with other cytochrome c peroxidases.

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Common phylogeny of catalase-peroxidases and ascorbate peroxidases

Cited by 50 publications

References 24 publications

Defenses against Oxidative Stress inNeisseria gonorrhoeae: a System Tailored for a Challenging Environment

Defenses against Oxidative Stress inNeisseria gonorrhoeae: a System Tailored for a Challenging Environment

A minor catalase/peroxidase from Burkholderia cenocepacia is required for normal aconitase activity

A Distinctive Electrocatalytic Response from the Cytochrome c Peroxidase of Nitrosomonas europaea

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