ANTIMYCIN-INSENSITIVE MUTANTS OF CANDIDA-UTILIS .2. EFFECTS OF ANTIMYCIN ON CYTOCHROME-B
ANTIMYCIN-INSENSITIVE MUTANTS OF CANDIDA-UTILIS .2. EFFECTS OF ANTIMYCIN ON CYTOCHROME-B
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DOI:
10.1016/0005-2728(75)90173-5
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发表时间:
1975-01-01
期刊:
影响因子:
--
通讯作者:
SLATER, EC
中科院分区:
文献类型:
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作者:
GRIMMELIKHUIJZEN, CJP;MARRES, CAM;SLATER, EC
1. Cytochromeb-562 is more reduced in submitochondrial particles of mutant 28 during the aerobic steady-state respiration with succinate than in particles of the wild type. When anaerobiosis is reached, the reduction of cytochromebis preceded by a rapid reoxidation in the mutant. A similar reoxidation is observed in the wild type in the presence of low concentrations of antimycin.2. In contrast to the wild type, inhibition of electron transport in the mutant has a much higher antimycin titre than effects on cytochromesb(viz., aerobic steadystate reduction; reduction in the presence of substrate, cyanide and oxygen; the ‘red shift’ and lowering ofE′0of cytochromeb-562). Moreover, the titration curve of electron transport is hyperbolic whereas the curves for the reduction are sigmoidal. The conclusion is, that in both mutant and wild type, the actions of antimycin on electron transport and cytochromesbare separable.3. The red shift in the mutant is more extensive than in the wild type.4. Cytochromeb-558 and cytochromeb-566 (that absorbs in mutant and wild type at 564.5 nm) do not respond simultaneously to addition of antimycin, indicating that they are two separate cytochromes.5. The difference between the effect of antimycin on electron transport and cytochromesbreduction is also found in intact cells of the mutant.6. A model is suggested for the wild-type respiratory chain in which (i) the cytochromesblie, in an uncoupled system, out of the main electron-transfer chain, (ii) antimycin induces a conformation change in QH2-cytochromecreductase resulting in effects on cytochromeband inhibition of electron transport, (iii) a second antimycinbinding site with low affinity to the antibiotic is present, capable of inhibiting electron transport.