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6 hydroxyquinoline/cereus
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Enzymatic properties of the membrane-bound NADH oxidase system in the aerobic respiratory chain of Bacillus cereus.
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Membranes prepared from Bacillus cereus KCTC 3674, grown aerobically on a complex medium, oxidized NADH exclusively, whereas deamino-NADH was little oxidized. The respiratory chain-linked NADH oxidase exhibited an apparent K(m) value of approximately 65 microM for NADH. The maximum activity of the
Electron transport system associated with membranes of Bacillus cereus during vegetative growth and sporulation.
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Membranes isolated from Bacillus cereus ATCC 4342 during vegetative growth and during sporulation contained cytochromes b, c and a + a(3) as well as flavoprotein as determined from reduced-minus-oxidized difference spectra. Although there appeared to be no qualitative change in the cytochromes,
HQNO-sensitive NADH:quinone oxidoreductase of Bacillus cereus KCTC 3674.
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The enzymatic properties of NADH:quinone oxidoreductase were examined in Triton X-100 extracts of Bacillus cereus membranes by using the artificial electron acceptors ubiquinone-1 and menadione. Membranes were prepared from B. cereus KCTC 3674 grown aerobically on a complex medium and oxidized with
A novel double heme substitution produces a functional bo3 variant of the quinol oxidase aa3 of Bacillus cereus. Purification and paratial characterization.
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A novel bo3-type quinol oxidase was highly purified from Bacillus cereus PYM1, a spontaneous mutant unable to synthesize heme A and therefore spectroscopically detectable cytochromes aa3 and caa3. The purified enzyme contained 12.4 nmol of heme O and 11.5 nmol of heme B mg-1 protein. The enzyme was
Bacillus cereus electron transport and proton motive force during aerotaxis.
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Aerotaxis (migration towards oxygen) of Bacillus cereus M63, a motile strain, was inhibited by potassium cyanide and 2-heptyl-4-hydroxyquinoline N-oxide, indicating a requirement for both the terminal oxidase (cytochrome aa3) and the cytochrome b segment of the electron transport system. The
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