Abstract
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=+140mV), cytochrome b-556 (E′ 0=+140mV) [or alternatively cytochrome b-563/556 (E′ 0=+140mV)] 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 α-band can be detected at 569 nm at 25°C and 565 nm at 77K.
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Abbreviations
- Hepes:
-
4-(2-hydroxyethyl)-1-piperazineethanesulphonic acid
- HQNO:
-
2-n-heptyl-4-hydroxyquinoline-N-oxide
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van Wielink, J.E., Reijnders, W.N.M., Oltmann, L.F. et al. Electron transport and cytochromes in aerobically grown Proteus mirabilis . Arch. Microbiol. 136, 152–157 (1983). https://doi.org/10.1007/BF00404791
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DOI: https://doi.org/10.1007/BF00404791