Bacterial Oxidation of Methane and Methanol

Anthony, Christopher

doi:10.1016/s0065-2911(08)60305-7

Cited by 299 publications

(209 citation statements)

References 204 publications

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“…A high hexulose phosphate synthase activity was present and the Entner-Doudoroff pathway of hexose phosphate dissimilation was operative as evidenced by the high specific activity of KDPG aldolase. As usual in methylotrophs, the Krebs' cycle is not used for catabolism (Anthony, 1986). However oxoglutarate dehydrogenase activity was found in extracts of fructosegrown cells.…”

Section: Methodsmentioning

confidence: 91%

Isolation and phenotypic characterization of methanol oxidation mutants of the restricted facultative methylotroph Methylophaga marina

Janvier

Frank

Luttik

et al. 1992

Journal of General Microbiology

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Methanol oxidation in Mefhyfophuga marina appears to be organized in a way similar to that in other Gramnegative methylotrophs, involving a quinoprotein methanol dehydrogenase (MDH; EC 1.1.99.8) and two soluble cytochromes. The MDH is composed of two different subunits, most probably arranged in an a2P2 structure. The two cytochromes are of the e-type and differ in size (molecular mass 19.5 and 12.5 kDa) and isoelectric point (PI 4.6 and 9.2). The one with the lowest isoelectric point, commonly designated as cytochrome eL, is able to oxidize reduced MDH. Taking advantage of the ability of M. marina, a restricted facultative methylotroph, to utilize fructose as a growth substrate, mutants impaired in methanol utilization were isolated after application of optimal concentrations of ethylmethane sulphonate. Three classes of methanol oxidation mutants were obtained. Class I mutants were affected in a global regulation of the synthesis of both apo-methanol-dehydrogenase and cytochrome cL as well as PQQ (pyrroloquinoline quinone). Class I1 mutants did not produce an active MDH, but instead a comparable amount of a 65 kDa protein was found in the cell-free extract upon SDS-PAGE. This mutant protein was purified and compared to wild-type MDH. It was located in the periplasm, but unlike MDH it was composed of only two identical large subunits. Each of these subunits was able to bind one molecule of PQQ. An antiserum raised against wild-type MDH did not react with the mutant protein. Conversely, an antiserum raised against mutant protein weakly cross-reacted with wild-type MDH, suggesting that the presence of the P-subunit in MDH dramatically changes its immunochemical behaviour. Three of the class I1 mutants did not produce PQQ. In the presence of PQQ, partial revertants able to grow on methanol medium were obtained (class 111). Class 111 mutants produced a stable apo-MDH consisting of a-and P-subunits and showing a normal reaction with the anti-MDH serum. Although this apo-MDH can bind PQQ, enzymic activity was not restored in nitro. This suggests that, in addition to apo-MDH and PQQ, other factors are required for the assembly of an enzymically active MDH.

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Section: Methodsmentioning

confidence: 91%

Isolation and phenotypic characterization of methanol oxidation mutants of the restricted facultative methylotroph Methylophaga marina

Janvier

Frank

Luttik

et al. 1992

Journal of General Microbiology

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“…It oxidizes methanol by way of the periplasmic quinoprotein methanol dehydrogenase (MDH) which interacts directly with a specific cytochrome c (called cytochrome cL). This then transfers electrons to a typical small cytochrome c (called cytochrome cH) which is the substrate for the membranebound oxidase cytochrome aa3 (for reviews see Anthony, 1982Anthony, ,1986Anthony, ,1988. In the first extensive study of the genes involved in methanol oxidation, 10 gene functions were described in M .…”

Section: Introductionmentioning

confidence: 99%

Characterization of a novel soluble c-type cytochrome in a moxD mutant of Methylobacterium extorquens AM1

Day

Nunn²,

Anthony³

1990

Journal of General Microbiology

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Methylobacterium extorquens AM1 contains a novel c-type cytochrome, called cytochrome c-553, previously thought to be a precursor of the electron acceptor (cytochrome cL) for methanol dehydrogenase. Its amino acid composition and serological characteristics show that it has no structural relationship to cytochrome cL. It usually comprises less than 5% of the total c-type cytochromes. In a moxD mutant, which contains neither methanol dehydrogenase nor cytochrome cL, it comprises 30% of the soluble cytochrome and it has been purified and characterized from that mutant. Cytochrome c-553 is large ( M , 23000), acidic and monohaem, with a redox potential of 194 mV. It reacts rapidly and completely with CO but is not autoxidizable. It is not autoreducible, and it is not an electron acceptor from methanol dehydrogenase or methylamhe dehydrogenase, nor an important electron donor to the oxidase. It is able to accept electrons from cytochrome cL and to donate electrons to cytochrome cH. It is present in the soluble fraction (presumably periplasmic) and membrane fraction of wild-type bacteria during growth on a wide range of growth substrates, but its function in these bacteria or in the moxD mutant has not been determined.

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“…pyrroloquinoline quinone (PQQ) dependent methanol dehydrogenase (MDH; EC 1.1.99.8) for the initial oxidation of methanol (Anthony 1982(Anthony , 1986Duine et al 1978Duine et al , 1986de Vries 1986). The situation in Gram-positive methylotrophic bacteria is less clear as relatively few of these organisms have been isolated and studied in detail thus far (Dijkhuizen and Levering 1987).…”

mentioning

confidence: 99%

Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme

et al. 1989

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Abstract. The enzymology of methanol utilization in thermotolerant methytotrophic Bacillus strains was investigated. In all strains an immunological]y related NAD-dependent methanol dehydrogenase was involved in the initial oxidation of methanol. In cells of Bacillus sp. C1 grown under methanol-limiting conditions this enzyme constituted a high percentage of total soluble protein. The methanol dehydrogenase from this organism was purified to homogeneity and characterized. In cell-free extracts the enzyme displayed biphasic kinetics towards methanol, with apparent Km values of 3.8 and 166 mM. Carbon assimilation was by way of the fructose-1,6-bisphosphate aldolase cleavage and transketolase/transaldolase rearrangement variant of the RuMP cycle of formaldehyde fixation. The key enzymes of the RuMP cycle, hexulose-6-phosphate synthase (HPS) and hexulose-6-phosphate isomerase (HPI), were present at very high levels of activity. Failure of whole cells to oxidize formate, and the absence of formaldehyde-and formate dehydrogenases indicated the operation of a non-linear oxidation sequence for formaldehyde via HPS. A comparison of the levels of methanol dehydrogenase and HPS in cells of Bacillus sp. C1 grown on methanol and glucose suggested that the synthesis of these enzymes is not under coordinate control.

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Bacterial Oxidation of Methane and Methanol

Cited by 299 publications

References 204 publications

Isolation and phenotypic characterization of methanol oxidation mutants of the restricted facultative methylotroph Methylophaga marina

Isolation and phenotypic characterization of methanol oxidation mutants of the restricted facultative methylotroph Methylophaga marina

Characterization of a novel soluble c-type cytochrome in a moxD mutant of Methylobacterium extorquens AM1

Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme

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