1990
DOI: 10.1093/oxfordjournals.jbchem.a123071
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A Novel aco-Type Cytochrome-c Oxidase from a Facultative Alkalophilic Bacillus: Purification, and Some Molecular and Enzymatic Features1

Abstract: A novel aco-type cytochrome-c oxidase was highly purified from the facultative alkalophilic bacterium, Bacillus YN-2000, grown at pH 10. The enzyme contained 9.0 nmol heme a/mg protein. It contained 1.23 mol of protoheme, 1.06 mol of heme c, 2.0 g atoms of copper, 2.5 g atoms of iron, and 1.8 g atoms of magnesium per mol of heme a. The enzyme molecule seemed to be composed of two subunits with Mrs of 52,000 and 41,600. On the basis of these results, the enzyme seemed to contain one molecule each of heme a, pro… Show more

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Cited by 31 publications
(21 citation statements)
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“…In this work, we report on the purification and characterization of a novel cytochrome bo 3 quinol oxidase from B. cereus PYM1. Our results indicate that the purified bo 3 oxidase is a promiscuous enzyme that arises from the simultaneous insertion of hemes B and O in the low and high spin sites, respectively, of the original aa 3 quinol oxidase apocytochrome. On the other hand, a functional promiscuous equivalent was not detected for the caa 3 apocytochrome in the PYM1 strain, thus suggesting that double heme substitution producing active variants is a rare event among oxidases.…”
mentioning
confidence: 75%
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“…In this work, we report on the purification and characterization of a novel cytochrome bo 3 quinol oxidase from B. cereus PYM1. Our results indicate that the purified bo 3 oxidase is a promiscuous enzyme that arises from the simultaneous insertion of hemes B and O in the low and high spin sites, respectively, of the original aa 3 quinol oxidase apocytochrome. On the other hand, a functional promiscuous equivalent was not detected for the caa 3 apocytochrome in the PYM1 strain, thus suggesting that double heme substitution producing active variants is a rare event among oxidases.…”
mentioning
confidence: 75%
“…Heme O is normally not present in the Bacillaceae family; however, the presence of heme O has been reported in wild type cells growing under limited aeration (3,4) or in mutants deficient in the ctaA gene that encodes for the oxygenase responsible for the conversion of heme O into heme A (i.e. Bacillus subtilis RB829R (14)) as well as, in other genetically uncharacterized (presumably ctaA) mutants (B. subtilis FG83 (15) and Bacillus cereus PYM1 (16)).…”
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confidence: 99%
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“…Bovine cardiac cytochrome c oxidase (Hartzell & Beinert, 1974), 7: thermophilus cytochrome ba, (Yoshida et al, 1984;Zimmerman et al, 1988), Bacillus YN-2000 cytochrome aco (Qureshi et al, 1990;Yumoto et al, 1993), rabbit serum HPX (Hrkal & Muller-Eberhard, 1971), and rabbit serum HPRG (Morgan, 1978) were purified as previously described. The aa3-600 ubiquinol oxidase was purified by the method of Lauraeus et al (1991) with minor modifications, from B. subtilis cells grown as described (Lauraeus et al, 1991).…”
Section: Methodsmentioning
confidence: 99%