Microbial Production of Carbon Monoxide from Flavonoids

Westlake, D. W. S.; Roxburgh, J. M.; Talbot, G.

doi:10.1038/189510a0

Cited by 96 publications

(37 citation statements)

References 8 publications

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“…strain JC1 can grow with 4.3 pimol of CO per liter of air (7), which indicates that it may utilize CO in highly polluted air (2.2 to 4.3 pumol/liter) in urban districts (48). It may also utilize CO in microenvironments in which a high concentration of CO is produced by decomposition of flavonoids and porphyrins (8,56).…”

Section: Discussionmentioning

confidence: 99%

Purification and some properties of carbon monoxide dehydrogenase from Acinetobacter sp. strain JC1 DSM 3803

Kim

1989

J Bacteriol

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A brown carbon monoxide dehydrogenase from CO-autotrophically grown cells of Acinetobacter sp. strain JC1, which is unstable outside the cells, was purified 80-fold in seven steps to better than 95% homogeneity, with a yield of 44% in the presence of the stabilizing agents iodoacetamide (1 mM) and ammonium sulfate (100 mM). The final specific activity was 474 iimol of acceptor reduced per min per mg of protein as determined by an assay based on the CO-dependent reduction of thionin. Methyl viologen, NAD(P), flavin mononucleotide, flavin adenine dinucleotide, and ferricyanide were not reduced by the enzyme, but methylene blue, thionin, and dichlorophenolindophenol were reduced. The molecular weight of the native enzyme was determined to be 380,000. Sodium dodecyl sulfate-gel electrophoresis revealed at least three nonidentical subunits of molecular weights 16,000 (a), 34,000 (if), and 85,000 (-y). The purified enzyme contained particulate hydrogenase-like activity. Selenium did not stimulate carbon monoxide dehydrogenase activity. The isoelectric point of the native enzyme was found to be 5.8; the Km of CO was 150 LM. The enzyme was rapidly inactivated by methanol. One mole of native enzyme was found to contain 2 mol of each of fiavin adenine dinucleotide and molybdenum and 8 mol each of nonheme iron and labile sulfide, which indicated that the enzyme was a molybdenum-containing iron-sulfur flavoprotein. The ratio of densities of each subunit after electrophoresis (a:p:ry = 1:2:6) and the number of each cofactor in the native enzyme suggest a a2iB2y2 structure of the enzyme. The carbon monoxide dehydrogenase of Acinetobacter sp. strain JC1 was found to have no immunological relationship with the enzymes-of Pseudomonas carboxydohydrogena and Pseudomonas carboxydovorans.Carbon monoxide dehydrogenase (CO-DH) is an enzyme responsible for the oxidation of CO in several gram-positive and -negative carboxydobacteria which are able to grow aerobically with CO as the sole source of carbon and energy (7, 14, 22, 31, 34-36, 39, 43, 58). Studies on the CO-DHs in the purified state, in partially purified preparations, and in extracts revealed that the enzymes from several carboxydobacteria are, with few exceptions, similar in biochemical and immunological properties (2, 6, 14, 22, 23, 25, 34-36, 39, 43).Acinetobacter sp. strain JC1 DSM 3803 is a new carboxydobacterium isolated from soil in Seoul, Korea (7). Preliminary studies with cell extracts showed that the CO-DH of this bacterium is an inducible enzyme which is loosely bound to the inner face of the cytoplasmic membrane (6, 18). The enzyme was found to be unstable outside the cell and to have no immunological relationship with that of Pseudomonas carboxydohydrogena (6), which implies the presence of a novel CO-DH in Acinetobacter sp. strain JC1.In this study, we examined purified CO-DH of Acinetobacter sp. strain JC1 in some detail to determine whether the basis for CO oxidation is diverse in the carboxydobacteria and to learn more about the process. Before the purificat...

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Section: Discussionmentioning

confidence: 99%

Purification and some properties of carbon monoxide dehydrogenase from Acinetobacter sp. strain JC1 DSM 3803

Kim

1989

J Bacteriol

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“…in soils (Conrad and Seiler 198Ob), and dark biological processes carried out by animals (Wittenberg 1960;Sjijstrand 1970), fungi (Simpson et al 1963;Westlake et al 1961), yeast (Radler et al 1974), hemolytic bacteria (Engel et al 1972, and marine bacteria (Junge et al 1971(Junge et al , 1972. The marine bacteria, belonging to the genera Alginomonas, Brevibacterium, and Agrobacterium are believed responsible for the CO supcrsaturation often observed in the dark zone of the oceans below 100 m (Junge et al 1971(Junge et al , 1972.…”

Section: Discussionmentioning

confidence: 99%

Production and consumption of carbon monoxide in a eutrophic lake1

Conrad

Aragno

Seiler³

1983

Limnology & Oceanography

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CO concentrationswere measured in the water of a eutrophic lake by a technique which allowed the detection of 30.5 nl CO* liter-l of water. In spring, when the lake was aerobic to the bottom, CO distribution was relatively homogeneous with concentrations of 40-130 nlaliter-l.In summer, CO concentrations ranged between 20 and 615 nleliter-' in the aerobic epilimnion and metalimnion, but reached values of >8,000 nl* liter-' in the anaerobic hypolimnion. CO increased during the morning and decreased during the afternoon in the upper water layers as well as in the dark hypolimnion.Incubation of lake water samples from different depths under daylight conditions resulted in a strong CO production. The lightdependent CO production was stimulated by the high numbers of Oscillatoria rubescens in the metalimnion, but also by material from the lake sediment. Incubation of lake water samples in darkness resulted in CO consumption under both aerobic and anaerobic conditions.

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“…It is known that CO is produced endogenously in normal man (24), and that approximately 1 mole of CO is produced per mole of heme catabolized (2, 1 1). CO formation has been described in algae (6,12,15), in fungi (23,33), and in higher plants (22,34). CO produced in the fungus, Aspergillus niger, has been shown to arise from the breakdown of rutin to phloroglucinol and protocatechuic acid (23).…”

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confidence: 99%

Formation of Carbon Monoxide and Bile Pigment in Red and Blue-Green Algae

Troxler

Dokos²

1973

Plant Physiol.

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Five blue-green and one red algal species produced carbon monoxide during photosynthetic growth. The blue-green algae synthesized CO and phycocyanobilin in equimolar quantities at identical rates. The red alga, Porphyridium cruentum, incorporated z-aminolevulinic acid-5-14C into phycoerythrobilin and CO. The ratio of the specific radioactivity of phycoerythrobilin to that of CO, and the kinetics and stoichiometry of phycocyanobilin and CO formation suggest that linear tetrapyrroles in plants are derived by the porphyrin pathway via the intermediate formation of heme. The similarity between bile pigment production in algae and in mammalian systems is discussed.Phycocyanobilin and phycoerythrobilin are linear tetrapyrroles covalently linked to apoproteins occurring in the photosynthetic apparatus of red, blue-green, and cryptomonad algae (17). These compounds are structurally related to bilirubin, the principal mammalian bile pigment derived from hemoglobin in senescent erythrocytes (1,14, 18,19). It is known that CO is produced endogenously in normal man (24), and that approximately 1 mole of CO is produced per mole of heme catabolized (2, 1 1). CO formation has been described in algae (6,12,15), in fungi (23, 33), and in higher plants (22,34). CO produced in the fungus, Aspergillus niger, has been shown to arise from the breakdown of rutin to phloroglucinol and protocatechuic acid (23). Nevertheless, in most reports concerning algae and higher plants, the metabolic origin of CO has not been established. We have shown that in the green algae, Cyanidium caldarium, CO is a by-product of phycocyanobilin formation (31). The present paper describes some quantitative and kinetic parameters of CO and bile pigment formation in five species of blue-green algae and in the red alga, Porphyridium cruentum.

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Microbial Production of Carbon Monoxide from Flavonoids

Cited by 96 publications

References 8 publications

Purification and some properties of carbon monoxide dehydrogenase from Acinetobacter sp. strain JC1 DSM 3803

Purification and some properties of carbon monoxide dehydrogenase from Acinetobacter sp. strain JC1 DSM 3803

Production and consumption of carbon monoxide in a eutrophic lake1

Formation of Carbon Monoxide and Bile Pigment in Red and Blue-Green Algae

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