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Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain.

Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain. Research Abstract Details 

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  • Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain. Abstract Text:

    a yaginumaA Yaginuma,s tsukitaS Tsukita,j sakamotoJ Sakamoto,n soneN Sone,

    The respiratory chain of Bacillus brevis was analyzed. Resting cells showed an H+/O ratio of 4.8-5.2 (5.01+/-0.26), when measured using an oxygen pulse method with endogenous substrates. This value is intermediate between those of Bacillus subtilis (about 4), which predominantly expresses cytochrome aa3-type quinol oxidase, and Bacillus stearothermophilus (about 6), which has quinol cytochrome c reductase plus caa3-type cytochrome c oxidase. Measurement of respiration with various substrates, and its inhibition by cyanide suggested that aa3-type quinol oxidase and caa3-type cytochrome c oxidase operate simultaneously in the respiratory chain of B. brevis. Both terminal oxidases were isolated by solubilizing B. brevis membranes with Triton X-100, and fractionating the extract using DEAE-Fractgel and gel-filtration columns. The quinol oxidase (aa3) was composed of four subunits (57, 34, 23, and 15 kDa), like its counterpart of B. subtilis, while three subunits (52, 34, and 22 kDa) were identified in the cytochrome c oxidase (caa3) preparation in B. stearothermophilus.

    Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain. Publishing Authors By Initials

    a yaginumaA Yaginuma,s tsukitaS Tsukita,j sakamotoJ Sakamoto,n soneN Sone,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

    PUBMED ID PMID:

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    Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 122

    Page Numbers: 969-76

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Nov

    YEAR: 1997

    Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain. Keywords Mesh Terms:

    KEYWORDS: Substrate Specificity

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain. Information

    Substance Name: Electron Transport Complex IV

    Registry Number: EC 1.9.3.1

    Grant and Affiliation Information for Characterization of two terminal oxidases in Bacillus brevis and efficiency of energy conservation of the respiratory chain.

    AFFILIATION: Department of Biochemical Engineering and Science, Kyushu Institute of Technology, Fukuoka.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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