Reduction of carbon monoxide to formaldehyde by the terminal oxidase of the marine bacterium <i>Pseudomonas nautica</i> strain 617

Arnaud, Sylvain; Malatesta, Francesco; Denis, Michel

doi:10.1016/0014-5793(92)80299-v

Cited by 3 publications

(1 citation statement)

References 17 publications

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“…This suggests that the cytochrome cbЈ oxidase possesses photolysis-dependent CO reductase activity that results in oxidation of redox proteins. Unusual CO reductase activity by which CO is converted to formaldehyde has been observed in the bbЈ oxidase of Pseudomonas nautica (2), in a reaction that is dependent on photolysis. To determine whether the cytochrome bbЈ oxidase of C. jejuni is capable of catalyzing CO reduction, formaldehyde, presumed to be generated by oxidase-mediated CO reduction, was assayed in whole cells and membranes of C. jejuni, but no significant levels were detectable in any fraction.…”

Section: Resultsmentioning

confidence: 99%

Oxygen Reactivity of Both Respiratory Oxidases in Campylobacter jejuni : the cydAB Genes Encode a Cyanide-Resistant, Low-Affinity Oxidase That Is Not of the Cytochrome bd Type

Elvers

Lee

et al. 2007

J Bacteriol

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The microaerophilic bacterium Campylobacter jejuni is a significant food-borne pathogen and is predicted to possess two terminal respiratory oxidases with unknown properties. Inspection of the genome reveals an operon (cydAB) apparently encoding a cytochrome bd-like oxidase homologous to oxidases in Escherichia coli and Azotobacter vinelandii. However, C. jejuni cells lacked all spectral signals characteristic of the high-spin hemes b and d of these oxidases. Mutation of the cydAB operon of C. jejuni did not have a significant effect on growth, but the mutation reduced formate respiration and the viability of cells cultured in 5% oxygen. Since cyanide resistance of respiration was diminished in the mutant, we propose that C. jejuni CydAB be renamed CioAB (cyanide-insensitive oxidase), as in Pseudomonas aeruginosa. We measured the oxygen affinity of each oxidase, using a highly sensitive assay that exploits globin deoxygenation during respiration-catalyzed oxygen uptake. The CioAB-type oxidase exhibited a relatively low affinity for oxygen (K m ‫؍‬ 0.8 M) and a V max of >20 nmol/mg/s. Expression of cioAB was elevated fivefold in cells grown at higher rates of oxygen provision. The alternative, ccoNOQP-encoded cyanide-sensitive oxidase, expected to encode a cytochrome cb-type enzyme, plays a major role in the microaerobic respiration of C. jejuni, since it appeared to be essential for viability and exhibited a much higher oxygen affinity, with a K m value of 40 nM and a V max of 6 to 9 nmol/mg/s. Lowtemperature photodissociation spectrophotometry revealed that neither oxidase has ligand-binding activity typical of the heme-copper oxidase family. These data are consistent with cytochrome oxidation during photolysis at low temperatures.

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Section: Resultsmentioning

confidence: 99%

Oxygen Reactivity of Both Respiratory Oxidases in Campylobacter jejuni : the cydAB Genes Encode a Cyanide-Resistant, Low-Affinity Oxidase That Is Not of the Cytochrome bd Type

Elvers

Lee

et al. 2007

J Bacteriol

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The carbon monoxide‐releasing molecule, corm‐3 (ru(co)₃cl(glycinate)), targets respiration and oxidases in campylobacter jejuni, generating hydrogen peroxide

et al. 2011

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SummaryCarbon monoxide (CO) is a classical respiratory inhibitor, but CO-releasing molecules (CO-RMs) have therapeutic value, increasing phagocytosis, and reducing sepsis-induced lethality. CORM-3, Ru(CO) 3 Cl(glycinate), a ruthenium-based carbonyl that liberates CO under physiological conditions, has previously been shown to inhibit bacterial growth and respiration, even at high concentrations of oxygen. Here, we report the effects of CORM-3 on the microaerophilic foodborne pathogen Campylobacter jejuni. Even at CO-RM (i.e., CO) concentrations that exceed dissolved oxygen levels, CORM-3 does not inhibit microaerobic growth. This insensitivity is not due to failure of CORM-3 to penetrate cells, as revealed by assay with extracellular myoglobin and by the ability of CO from externally added CORM-3 to bind intracellular membrane-associated respiratory oxidases. Even at almost 200 lM oxygen, CORM-3 inhibits formate-dependent respiration and leads to generation of hydrogen peroxide. This work shows that CO-RMs have valuable properties as antimicrobial agents; however, growth inhibition does not always accompany inhibition of respiration, even when ambient oxygen concentrations are low.

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Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: Heme d binds CO with high affinity

Borisov

2008

Biochemistry Moscow

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Comparative studies on the interaction of the membrane-bound and detergent-solubilized forms of the enzyme in the fully reduced state with carbon monoxide at room temperature have been carried out. CO brings about a bathochromic shift of the heme d band with a maximum at 644 nm and a minimum at 624 nm, and a peak at 540 nm. In the Soret band, CO binding to cytochrome bd results in absorption decrease and minima at 430 and 445 nm. Absorption perturbations in the Soret band and at 540 nm occur in parallel with the changes at 630 nm and reach saturation at 3-5 microM CO. The peak at 540 nm is probably either beta-band of the heme d-CO complex or part of its split alpha-band. In both forms of cytochrome bd, CO reacts predominantly with heme d. Addition of high CO concentrations to the solubilized cytochrome bd results in additional spectral changes in the gamma-band attributable to the reaction of the ligand with 10-15% of low-spin heme b558. High-spin heme b595 does not bind CO even at high concentrations of the ligand. The apparent dissociation constant values for the heme d-CO complex of the membrane-bound and detergent-solubilized forms of the fully reduced enzyme are about 70 and 80 nM, respectively.

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Reduction of carbon monoxide to formaldehyde by the terminal oxidase of the marine bacterium Pseudomonas nautica strain 617

Cited by 3 publications

References 17 publications

Oxygen Reactivity of Both Respiratory Oxidases in Campylobacter jejuni : the cydAB Genes Encode a Cyanide-Resistant, Low-Affinity Oxidase That Is Not of the Cytochrome bd Type

Oxygen Reactivity of Both Respiratory Oxidases in Campylobacter jejuni : the cydAB Genes Encode a Cyanide-Resistant, Low-Affinity Oxidase That Is Not of the Cytochrome bd Type

The carbon monoxide‐releasing molecule, corm‐3 (ru(co)₃cl(glycinate)), targets respiration and oxidases in campylobacter jejuni, generating hydrogen peroxide

Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: Heme d binds CO with high affinity

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Reduction of carbon monoxide to formaldehyde by the terminal oxidase of the marine bacterium Pseudomonas nautica strain 617

Cited by 3 publications

References 17 publications

Oxygen Reactivity of Both Respiratory Oxidases in Campylobacter jejuni : the cydAB Genes Encode a Cyanide-Resistant, Low-Affinity Oxidase That Is Not of the Cytochrome bd Type

Oxygen Reactivity of Both Respiratory Oxidases in Campylobacter jejuni : the cydAB Genes Encode a Cyanide-Resistant, Low-Affinity Oxidase That Is Not of the Cytochrome bd Type

The carbon monoxide‐releasing molecule, corm‐3 (ru(co)3cl(glycinate)), targets respiration and oxidases in campylobacter jejuni, generating hydrogen peroxide

Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: Heme d binds CO with high affinity

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The carbon monoxide‐releasing molecule, corm‐3 (ru(co)₃cl(glycinate)), targets respiration and oxidases in campylobacter jejuni, generating hydrogen peroxide