<i>o</i>‐Type cytochrome oxidase in the membrane of aerobically grown <i>Pseudomonas aeruginosa</i>

Matsushita, Kazunobu; Shinagawa, Emiko; Adachi, Osao; Ameyama, Minoru

doi:10.1016/0014-5793(82)80864-8

Cited by 70 publications

(44 citation statements)

References 17 publications

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“…Oxidation of these substrates was very sensitive to azide, the inhibition being of the noncompetitive type. The rates of oxidation of cytochrome c and TMPD by the partially-purified oxidase are similar to those measured with the cytochromes co of Rhodopseudornonas palustris (King & Drews, 1976), Pseudornonas aeruginosa (Matsushita et al, 1982) and Methylophilus rnethylotrophus (Carver & Jones, 1983;Froud & Anthony, 1984). All these results suggest that o-type oxidase solubilized from the membranes is of the cytochrome co type.…”

Section: Discussionsupporting

confidence: 75%

“…Much less is known about the second class of o-type oxidase, cytochrome co, although it has been purified from a number of bacteria, including Methylophilus rnethylotrophus (Carver & Jones, 1983;Froud & Anthony, 1984), Azotobacter vinelandii (Yang & Jurtshuk, 1978;Jurtshuk et al, 1981;Hunter et al, 1989), Rhodopseudornonas palustris (King & Drews, 1976), and Pseudornonas aeruginosa (Matsushita et al, 1982). Cytochrome co is sensitive to low concentrations of azide and cyanide, and it oxidizes the high-potential substrates cytochrome c and ascorbate/TMPD, but not the lowpotential substrate ubiquinol.…”

Section: H T C Chan and C Anthonymentioning

confidence: 99%

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The o-type oxidase of the acidophilic methylotroph Acetobacter methanolicus

Chan

Anthony

1991

Journal of General Microbiology

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Membranes of the acidophilic methylotroph Acetobucter methanolicus contained only b-and c-type cytochrome and a CO-binding b-type cytochrome. An azide-sensitive oxidase that oxidizes cytochrome c and ascorbatel TMPD was solubilized from the membrane with a mixture of CHAPS and Zwittergent3-12 (1.7 fold increase in specific activity with 32% yield). The solubilized oxidase is unusually stable with respect to high ionic strength (200 mM-NaC1) and stable between pH 4.0 and 6.8. Of the two soluble c-type cytochromes from A. methanoficus only the typical class I cytochrome (cytochrome cH) was a good substrate, as was equine cytochrome c. The oxidase was partially purified by anion-exchange chromatography but further purification proved impossible. The yield with respect to equine cytochrome c oxidation was l8%, with a 22-fold purification, but during purification most of the activity with respect to cytochrome cH and TMPD was lost. Neutral phospholipids had little effect on activity of the oxidase but the charged phospholipids phosphatidylglycerol and phosphatidylserine stimulated activity up to about fourfold. It proved impossible to incorporate the oxidase into active lipoprotein vesicles. During the purification process the pH optimum for oxidation of cytochrome cH was unchanged (pH 5.6) whereas that for oxidation of equine cytochrome changed from pH 9.5 to 7.5 and the sensitivity of the oxidase to azide changed from non-competitive to competitive during the purification process. The partially-purified oxidase contained only btype cytochrome, some of which was CO-reactive. It is proposed that the oxidase is a cytochrome co type of oxidase that loses its cytochrome c component during the purification process and is only able to oxidize c-type cytochromes if these can be formed into a 'reconstituted' cytochrome co with the partially-purified oxidase. IntroductionThe present paper describes work on an unusual o-type oxidase from the acidophilic methylotroph Acetobacter methanolicus, which grows at pH 4 on methanol as its sole carbon and energy source (Steudel & Babel, 1982;Steudel et al., 1980). As in other methylotrophic bacteria, methanol is oxidized by way of the quinoprotein methanol dehydrogenase, its specific electron acceptor cytochrome cL, and a typical class I c-type cytochrome which is oxidized by a membrane oxidase (Anthony, 1982(Anthony, , 1986Elliott & Anthony, 1988). Except for the oxidase all these proteins are periplasmic and so operate at pH4, the pH of the growth medium. Preliminary observations suggested that this oxidase may be more stable to extremes of pH and salt concentration compared with cytochrome oxidases in other bacteria.The bacterial o-type oxidases are defined loosely as oxidases having a CO-binding cytochrome b, which for convenience is usually referred to as cytochrome o and which is assumed to be the oxygen-reactive site. Cytochrome o was first described in Staphylococcus aureus (Chance, 1953 ;Castor & Chance, 1959) and the 0-type oxidases have since been shown to be the most widely...

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Section: Discussionsupporting

confidence: 75%

Section: H T C Chan and C Anthonymentioning

confidence: 99%

The o-type oxidase of the acidophilic methylotroph Acetobacter methanolicus

Chan

Anthony

1991

Journal of General Microbiology

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“…Cytochrome co is a cytochrome c oxidase that may be related to the cytochrome cbb 3 -type oxidase of the haem-copper superfamily (Matsushita et al, 1982;Thö ny-Meyer et al, 1994). The second is a cyanide-insensitive oxidase (CIO) of unknown molecular composition.…”

Section: Introductionmentioning

confidence: 99%

The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide‐insensitive terminal oxidase related to the cytochrome bd quinol oxidases

Cunningham

Pitt

Williams

1997

Molecular Microbiology

122

151

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SummaryThe structural genes for the cyanide-insensitive terminal oxidase (CIO) of Pseudomonas aeruginosa were sequenced. The locus comprised two open reading frames, cioA and cioB, coding for gene products of 488 and 335 amino acid residues with predicted molecular masses of 54 241 and 37 016 Da respectively. These genes were encoded by a 2.7 kb transcript and probably comprise an operon. Upstream of a major transcriptional start site is a ¹10 promoter region and, approximately at nucleotides ¹50 and þ13, there are sequences homologous to the binding site of the transcriptional regulator Anr. The deduced amino acid sequences of CioA and CioB are homologous to the cytochrome bd quinol oxidases of Escherichia coli and Azotobacter vinelandii. However, no cytochrome d -like signals were found in wild-type P. aeruginosa strains. An atypical cytochrome d -like signal was seen under low-aeration growth conditions but only in strains in which the cioAB genes were present on a high-copy-number plasmid. The appearance of these cytochrome d -like signals was not paralleled by a concomitant increase in CIO activity. These data support the hypothesis that the CIO of P. aeruginosa does not contain haem d. This raises the possibility that there is a family of bacterial quinol oxidases related to the cytochrome bd of E. coli that can differ in their haem composition from the E. coli paradigm.

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“…3 ,4) The ethanol oxidase respiratory chain has been studied in several acetic acid bacteria and shown to consist of ADH, ubiquinone, and either cytochrome ba or cytochrome bo ubiquinol oxidase. 3 ,4.15 18) In this work we describe a more effective new purification procedure for ADH from A. methanolicus. Kinetic properties of this ADH using artificial electron acceptors such as potassium ferricyanide, DCIP, PMS, and ubiqu.lnones-l (QI) and 2 (Q2) were investigated.…”

mentioning

confidence: 99%