A cb-type cytochrome-c oxidase terminates the respiratory chain in Helicobacter pylori.
Abstract: A Helicobacter pylori membrane fraction oxidized yeast and equine cytochrome c, and N,N,N',N'-tetramethyl-p-phenylenediamine (TMPD). When ascorbate was used as reductant, the Vmax and apparent Km values were 612 nmol electron min-1 (mg protein)-1 and 14 microM for yeast, and 419 nmol electron min-1 (mg protein)-1 and 19 microM for equine cytochrome c, respectively. For TMPD oxidation, the Vmax and Km values were 640 nmol electron min-1 (mg protein)-1 and 182 microM, respectively. These oxidase activities showed a high affinity for oxygen. Inhibition of both cytochrome-c and TMPD oxidase activities by 50% was caused by about 4 microM cyanide and about 0.5 mM azide. Redox difference spectra of the membrane solubilized with Triton X-100 showed b- or c-type cytochromes but not aa3-type cytochromes. c-type and a part of some b-type cytochromes were reduced with ascorbate plus TMPD. A CO difference spectrum revealed that protohaem, but not an aa3-type cytochrome, may be interacting with CO/oxygen. Only protohaem was detected in the haem fraction extracted from the membrane. Three polypeptides (60, 38 and 29 kDa) were found to be bearing haem c after SDS-PAGE of the membrane. From these results, it was suggested that the cbb3-type cytochrome-c oxidase, having a haem-copper binuclear centre like the cytochrome aa3-type oxidase, but differing in a few other properties, functions as a terminal oxidase in the respiratory chain of H. pylori.
Publication Date: 1996-07-01 PubMed ID: 8757739DOI: 10.1099/13500872-142-7-1757Google Scholar: Lookup
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- Journal Article
Summary
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The research article focuses on the exploration of how a cb-type cytochrome-c oxidase, which is a type of enzyme, influences the final stages of the respiratory chain in a bacterium known as Helicobacter pylori. The study identifies the specifics of this process, indicating the oxidase’s high affinity for oxygen and its reactions with various compounds and/or substances.
Understanding the Oxidation Process
- The research first analyzed the oxidation process in a Helicobacter pylori membrane fraction when responding to yeast and equine cytochrome c, and a substance known as TMPD.
- The rate and strength of the oxidation reaction were measured when ascorbate was used as a reductant, a substance that donates electrons in the oxidation-reduction process.
- This showed that these oxidase activities were highly attracted to oxygen.
Effects of Different Inhibitors
- Examinations were conducted to observe the effects when both cytochrome-c and TMPD oxidase activities were inhibited by two different substances, cyanide and azide, showing a 50% decrease in their activities.
- This presented important findings regarding the factors that could potentially halt or slow the oxidation process.
Exploration of the Redox Difference Spectra
- The researchers used a process known as a redox difference spectrum to analyze the membrane solubilized with Triton X-100, identifying the presence of different types of cytochromes.
- This helped to further indicate the specific types of cytochromes that were interacting with CO/oxygen.
Finding the Terminal Oxidase
- The presence of protohaem, and not an aa3-type cytochrome, in the haem fraction extracted from the membrane, and the detection of three polypeptides bearing haem c indicated a new finding.
- These results suggested that the cbb3-type cytochrome-c oxidase, although similar to the cytochrome aa3-type oxidase in having a haem-copper binuclear centre, differed in a few other properties, and acted as a terminal oxidase in the respiratory chain of H. pylori.
Cite This Article
APA
Nagata K, Tsukita S, Tamura T, Sone N.
(1996).
A cb-type cytochrome-c oxidase terminates the respiratory chain in Helicobacter pylori.
Microbiology (Reading), 142 ( Pt 7), 1757-1763.
https://doi.org/10.1099/13500872-142-7-1757 Publication
Researcher Affiliations
- Department of Bacteriology, Hyogo College of Medicine, Nishinomiya, Japan.
MeSH Terms
- Animals
- Electron Transport
- Electron Transport Complex IV / chemistry
- Electron Transport Complex IV / metabolism
- Helicobacter pylori / metabolism
- Heme / chemistry
- Horses
- In Vitro Techniques
- Kinetics
- Membranes / metabolism
- Oxidation-Reduction
- Oxygen Consumption
- Saccharomyces cerevisiae / enzymology
- Spectrophotometry
- Tetramethylphenylenediamine / metabolism
Citations
This article has been cited 18 times.- Jaramillo-Lanchero RD, Suarez-Alvarez P, Teheran-Sierra L. Effect of respiratory inhibitors and quinone analogues on the aerobic electron transport system of Eikenella corrodens.. Sci Rep 2021 Apr 26;11(1):8987.
- Kelley BR, Lu J, Haley KP, Gaddy JA, Johnson JG. Metal homeostasis in pathogenic Epsilonproteobacteria: mechanisms of acquisition, efflux, and regulation.. Metallomics 2021 Jan 16;13(1).
- Hirai T, Osamura T, Ishii M, Arai H. Expression of multiple cbb(3) cytochrome c oxidase isoforms by combinations of multiple isosubunits in Pseudomonas aeruginosa.. Proc Natl Acad Sci U S A 2016 Nov 8;113(45):12815-12819.
- Haley KP, Gaddy JA. Metalloregulation of Helicobacter pylori physiology and pathogenesis.. Front Microbiol 2015;6:911.
- Arai H, Kawakami T, Osamura T, Hirai T, Sakai Y, Ishii M. Enzymatic characterization and in vivo function of five terminal oxidases in Pseudomonas aeruginosa.. J Bacteriol 2014 Dec;196(24):4206-15.
- Tavares AF, Parente MR, Justino MC, Oleastro M, Nobre LS, Saraiva LM. The bactericidal activity of carbon monoxide-releasing molecules against Helicobacter pylori.. PLoS One 2013;8(12):e83157.
- Xie H, Buschmann S, Langer JD, Ludwig B, Michel H. Biochemical and biophysical characterization of the two isoforms of cbb3-type cytochrome c oxidase from Pseudomonas stutzeri.. J Bacteriol 2014 Jan;196(2):472-82.
- Atack JM, Srikhanta YN, Djoko KY, Welch JP, Hasri NH, Steichen CT, Vanden Hoven RN, Grimmond SM, Othman DS, Kappler U, Apicella MA, Jennings MP, Edwards JL, McEwan AG. Characterization of an ntrX mutant of Neisseria gonorrhoeae reveals a response regulator that controls expression of respiratory enzymes in oxidase-positive proteobacteria.. J Bacteriol 2013 Jun;195(11):2632-41.
- Arai H. Regulation and Function of Versatile Aerobic and Anaerobic Respiratory Metabolism in Pseudomonas aeruginosa.. Front Microbiol 2011;2:103.
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- Schweinitzer T, Mizote T, Ishikawa N, Dudnik A, Inatsu S, Schreiber S, Suerbaum S, Aizawa S, Josenhans C. Functional characterization and mutagenesis of the proposed behavioral sensor TlpD of Helicobacter pylori.. J Bacteriol 2008 May;190(9):3244-55.
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