Molecular characterization of the membrane‐bound quinol peroxidase functionally connected to the respiratory chain

Yamada, Hiroyuki; Takashima, Eizo; Kawai, Kiyoshi

doi:10.1111/j.1742-4658.2006.05637.x

Cited by 21 publications

(41 citation statements)

References 60 publications

(85 reference statements)

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“…Hydropathy analysis revealed that there is one possible membrane-spanning segment at the N-terminal (data not shown), which is responsible for association with the inner membrane. Although the N-terminal about 20-amino-acid sequence has a character of basic amino acids followed by a hydrophobic sequence, similar to that of a signal sequence, it may be not removed because a similar sequence is present in purified tri-heme CCP in A. actinomycetemcomitans [Yamada et al, 2007;Takashima et al, 2008]. This is consistent with the finding that most peroxidase activity in Z. mobilis was recovered in membrane fractions (see below).…”

Section: Structural Characteristics Of Zmcytcsupporting

confidence: 79%

“…ZmCytC in Z. mobilis has been annotated as CCP [Seo et al, 2005], though it seems to possess three heme cbinding motifs similar to ubiquinol peroxidase in A. actinomycetemcomitans [Yamada et al, 2007;Takashima et al, 2008]. In order to determine the physiological function of ZmCytC and its electron donor, ZmcytC -disrupted mutant was constructed and examined.…”

Section: Discussionmentioning

confidence: 99%

“…ZmCytC shares 39-43% sequence identity with di-heme CCPs and 44-57% with tri-heme CCPs. Yamada et al [2007] reported that the tri-heme CCP in A. actinomycetemcomitans is ubiquinol peroxidase, which is very similar in primary sequence to ZmCytC (47% identity). These findings strongly suggest that ZmCytC is a member of a tri-heme CCP family.…”

Section: Structural Characteristics Of Zmcytcmentioning

confidence: 99%

“…They bear an N-terminal extension with a heme c -binding motif (CXXCH) and a putative methionine ligand [Atack and Kelly, 2007]. The tri-heme CCP in Actinomyces actinomycetemcomitans has been demonstrated to be a quinol peroxidase based on evidence that it utilizes reduced ubiquinone-1 as an electron donor for the reduction of H 2 O 2 to water [Yamada et al, 2007;Takashima et al, 2008].…”

Section: Introductionmentioning

confidence: 99%

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Physiological Importance of Cytochrome c Peroxidase in Ethanologenic Thermotolerant Zymomonas mobilis

et al. 2011

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Zymomonas mobilis ZmCytC as a peroxidase bearing three heme c-binding motifs was investigated with ΔZmcytC constructed. The mutant exhibited filamentous shapes and reduction in growth under a shaking condition at a high temperature compared to the parental strain and became hypersensitive to exogenous H₂O₂. Under the same condition, the mutation caused increased expression of genes for three other antioxidant enzymes. Peroxidase activity, which was detected in membrane fractions with ubiquinol-1 as a substrate but not with reduced horse heart cytochrome c, was almost abolished in ΔZmcytC. Peroxidase activity was also detected with NADH as a substrate, which was significantly inhibited by antimycin A. NADH oxidase activity of ΔZmcytC was found to be about 80% of that of the parental strain. The results suggest the involvement of ZmCytC in the aerobic respiratory chain via the cytochrome bc₁ complex in addition to the previously proposed direct interaction with ubiquinol and its contribution to protection against oxidative stress.

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Section: Structural Characteristics Of Zmcytcsupporting

confidence: 79%

Section: Discussionmentioning

confidence: 99%

Section: Structural Characteristics Of Zmcytcmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Physiological Importance of Cytochrome c Peroxidase in Ethanologenic Thermotolerant Zymomonas mobilis

et al. 2011

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“…The qpo gene encoding quinol peroxidase was also identified. The qpo gene is highly similar to ccpR, but the deduced amino acid sequence of qpo has three haem c-binding motifs while that of ccpR has two motifs (Yamada et al, 2007). The expression level of qpo was higher in cells grown on ethanol or the mix of ethanol and glucose, but significantly reduced in those grown on glucose (Fig.…”

Section: Differential Expression Of the Highly Branched Respiratory Cmentioning

confidence: 95%

Transcriptome response to different carbon sources in Acetobacter aceti

et al. 2011

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The draft genome sequence of Acetobacter aceti NBRC 14818 was determined by wholegenome shotgun sequencing and the transcriptome profile in cells exponentially grown on ethanol, acetate or glucose was analysed by using a DNA microarray. The genes for all enzymes that constitute the complete tricarboxylic acid (TCA) cycle and glyoxylate pathway were identified in the genome. The TCA cycle genes showed higher expression levels in A. aceti cells grown on acetate or glucose and the glyoxylate pathway genes were significantly induced by ethanol or acetate. Many SOS-response genes were upregulated in cells grown on ethanol, indicating that ethanol provoked damage of DNA and proteins. The superoxide dismutase and catalase genes showed high expression levels in culture on glucose, indicating that oxidation of glucose induced oxidative stress. A. aceti NBRC 14818 was found to have a highly branched respiratory chain. The genes for two type I and one type II NADH dehydrogenase were identified. The genes for one of the type I enzymes were highly expressed when cells were grown on acetate or glucose, but were significantly downregulated in culture on ethanol, probably because ubiquinones were directly reduced by pyrroloquinoline quinone-dependent alcohol dehydrogenase. Four sets of the genes for quinol oxidases, one bo 3 -type (BO3), one bd-type and two cyanide-insensitive-types (CIOs), were identified in the genome. The genes for BO3, which might have proton-pumping activity, were highly expressed under the conditions tested, but were downregulated in the glucose culture. In contrast, the genes for one of the CIOs were significantly upregulated in cells grown on glucose. The two CIOs, which are expected to have lower energy-coupling efficiency, seemed to have a higher contribution in glucose-grown cells. These results indicate that energy conservation efficiency is fine-tuned by changing the respiratory components according to the growth conditions in A. aceti cells.

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Physiological Roles of a Periodontopathic Bacterial Membrane-Bound Quinol Peroxidase

Kawai

2013

Studies on Periodontal Disease

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Molecular characterization of the membrane‐bound quinol peroxidase functionally connected to the respiratory chain

Cited by 21 publications

References 60 publications

Physiological Importance of Cytochrome <i>c</i> Peroxidase in Ethanologenic Thermotolerant <i>Zymomonas mobilis</i>

Physiological Importance of Cytochrome <i>c</i> Peroxidase in Ethanologenic Thermotolerant <i>Zymomonas mobilis</i>

Transcriptome response to different carbon sources in Acetobacter aceti

Physiological Roles of a Periodontopathic Bacterial Membrane-Bound Quinol Peroxidase

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