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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 The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- 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 19 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.
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- 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.
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