Electron transport and cytochromes in aerobically grown Proteus mirabilis

The function of the cytochromes in electron transport from NADH to oxygen in aerobically grown Proteus mirabilis has been determined. 77K-Spectra of cytoplasmic membrane suspensions, frozen while catalyzing electron transport from NADH to oxygen, in the presence as well as in the absence of 2-n-hept...

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Published in:Archives of microbiology 1983-11, Vol.136 (2), p.152-157
Main Authors: VAN WIELINK, J. E, REIJINDERS, W. N. M, OLTMANN, L. F, STOUTHAMER, A. H
Format: Article
Language:English
Subjects:
Bacteriology
Biological and medical sciences
Cytochrome b Group - metabolism
Cytochromes - metabolism
Electron Transport
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
NAD - metabolism
Oxidation-Reduction
Oxygen Consumption
Proteus mirabilis - metabolism
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Summary:The function of the cytochromes in electron transport from NADH to oxygen in aerobically grown Proteus mirabilis has been determined. 77K-Spectra of cytoplasmic membrane suspensions, frozen while catalyzing electron transport from NADH to oxygen, in the presence as well as in the absence of 2-n-heptyl-4-hydroxyquinoline-N-oxide, have been recorded. Analysis of these 77K-spectra revealed that cytochrome b-563 (E'0 = +140 mV), cytochrome b-556 (E'0 = +140 mV) [or alternatively cytochrome b-563/556 (E'0 = +140 mV)] and cytochrome b-557 (E'0 = +50 mV) may function in a Q or b-cycle. The function of cytochrome c-549 (E'0 = +75 mV), which seems to be present only in a very low concentration, and cytochrome b-556 (E'0 = -105 mV), which reacts very slowly to the addition of NADH and oxygen, remains unclear. Cytochrome o, the main oxidase of aerobically grown P. mirabilis cells, can not be detected by the methods described above. Only when the reduced form of cytochrome o is liganded with carbon monoxide a specific alpha-band can be detected at 569 nm at 25 degrees C and 565 nm at 77K.
ISSN:0302-8933
1432-072X
DOI:10.1007/BF00404791