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

Journal of Biochemistry
A YaginumaN Sone

Abstract

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.

Citations

Mar 23, 2010·Journal of Bioenergetics and Biomembranes·Kazuaki YoshimuneIsao Yumoto
Mar 23, 2012·Journal of Bioenergetics and Biomembranes·Toshikazu HirabayashiIsao Yumoto
Feb 25, 2014·Antonie van Leeuwenhoek·Amrita Kumari PandaAshok Kumar Panigrahi
Jan 11, 2016·Journal of Bioenergetics and Biomembranes·Toshitaka GotoIsao Yumoto
Jun 15, 2010·Journal of Bioscience and Bioengineering·Jun-ichi KishikawaJunshi Sakamoto
Apr 6, 2005·Biochemistry. Biokhimii︠a︡·M S MuntyanV S Ustiyan

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