Abstract:
:The terminal oxidase content of Bacillus firmus OF4, a facultative alkaliphile that grows well over the pH range of 7.5 to 10.5, was studied by difference spectroscopy. Evidence was found for three terminal oxidases under different growth conditions. The growth pH and the stage of growth profoundly affected the expression of one of the oxidases, cytochrome d. The other two oxidases, cytochrome caa3 and cytochrome o, were expressed under all growth conditions tested, although the levels of both, especially cytochrome caa3, were higher at more alkaline pH (P.G. Quirk, A.A. Guffanti, R.J. Plass, S. Clejan, and T.A. Krulwich, Biochim. Biophys. Acta, in press). These latter oxidases were identified in everted membrane vesicles by reduced-versus-oxidized difference spectra (absorption maximum at 600 nm for cytochrome caa3) and CO-reduced-versus-reduced difference spectra (absorption maxima at 574 and 414 nm for cytochrome o). All three terminal oxidases were solubilized from everted membranes and partially purified. The difference spectra of the solubilized, partially purified cytochrome caa3 and cytochrome o complexes were consistent with these assignments. Cytochrome d, which has not been identified in a Bacillus species before, was tentatively assigned on the basis of its absorption maxima at 622 and 630 nm in reduced-versus-oxidized and CO-reduced-versus-reduced difference spectra, respectively, resembling the maxima exhibited by the complex found in Escherichia coli. The B. firmus OF4 cytochrome d was reducible by NADH but not by ascorbate-N,N,N',N'-tetramethyl-p-phenylenediamine in everted membrane vesicles. Cytochrome d was expressed under two conditions: in cells growing exponentially at pH 7.5 (but not at pH 10.5) and in cells stationary phase at either pH 7.5 or 10.5. Protein immunoblots with antibodies against subunit I of the E. coli cytochrome d complex reacted only with membrane vesicles that contained spectrally identifiable cytochrome d. Additional evidence that this B. firmus OF4 cytochrome is related to the E. coli complex was obtained with a solubilized, partially purified fraction of cytochrome d that also reacted with antibodies against the subunits of the E. coli cytochrome d.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Hicks DB,Plass RJ,Quirk PGdoi
10.1128/jb.173.16.5010-5016.1991keywords:
subject
Has Abstractpub_date
1991-08-01 00:00:00pages
5010-6issue
16eissn
0021-9193issn
1098-5530journal_volume
173pub_type
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1979-12-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1982-09-01 00:00:00
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更新日期:1996-03-01 00:00:00
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更新日期:1980-03-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.154.1.429-436.1983
更新日期:1983-04-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章,评审
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更新日期:1973-02-01 00:00:00
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更新日期:1979-11-01 00:00:00
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doi:10.1128/JB.134.3.808-820.1978
更新日期:1978-06-01 00:00:00
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journal_title:Journal of bacteriology
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doi:10.1128/JB.98.3.943-946.1969
更新日期:1969-06-01 00:00:00
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journal_title:Journal of bacteriology
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更新日期:2013-10-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章,评审
doi:10.1128/jb.175.6.1555-1560.1993
更新日期:1993-03-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.176.17.5513-5524.1994
更新日期:1994-09-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1971-10-01 00:00:00