The structure and mechanism of methanol dehydrogenase

Anthony, Christopher; Williams, Paul A.

doi:10.1016/s1570-9639(03)00042-6

Cited by 140 publications

(140 citation statements)

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“…This MD derived structure is not in accord with the following: (i) the suggestion that Asp-297-CO 2 Ϫ serves as the general-base catalyst (14)(15)(16)(17); and (ii) that the oxidation takes place, not by hydride transfer, but by an addition elimination reaction (18,19) (Scheme 1, in which the general base may be Glu-171-CO 2 Ϫ or Asp-297-CO 2 Ϫ ). The MD studies (6,7,9) showed that Asp-297-CO 2 Ϫ is not in position to act as a generalbase catalyst for the oxidation of MeOH by MDH.…”

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confidence: 88%

Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase

Zhang

Reddy

Bruice

2007

Proc. Natl. Acad. Sci. U.S.A.

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hydride transfer ͉ molecular dynamics ͉ pyrroloquinoline quinone W e have had a long standing interest in the mechanism of o-quinone cofactor and model reactions (for examples, see refs. 1-4). More recently, our attention has been directed to the employment of computational methods, particularly in the mechanism of the oxidation of methanol and glucose by the appropriate quinoprotein enzymes (5-11).The present study concerns bacterial quinoprotein methanol dehydrogenase (MDH) catalysis of the oxidation of CH 3 OH 3 CH 2 O by the pyrroloquinoline quinone (PQQ) cofactor. MDH is a hetrotetramer with two heavy and two light subunits. The catalytic chemistry is located in the heavy subunits. The crystal structure (PDB code 1G72; ref. 10) of the reduced PQQ bound to MDH presents Wat1 hydrogen bonding to the -CO 2

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mentioning

confidence: 88%

Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase

Zhang

Reddy

Bruice

2007

Proc. Natl. Acad. Sci. U.S.A.

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“…In all three phyllosphere samples, enzymes involved in aerobic methylotrophy prevailed, whereby the large subunit of methanol dehydrogenase (MxaF) (Anthony and Williams, 2003), methanol dehydrogenase-like protein XoxF (Schmidt et al, 2010) and formaldehydeactivating enzyme Fae (Vorholt et al, 2000) were among the most frequently detected proteins in the metaproteomes. They were assigned to the genus Methylobacterium, a dominant member of the bacterial phyllosphere community.…”

Section: Metaproteogenomics Of the Rice Microbiota C Knief Et Almentioning

confidence: 99%

Metaproteogenomic analysis of microbial communities in the phyllosphere and rhizosphere of rice

et al. 2011

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The above-and below-ground parts of rice plants create specific habitats for various microorganisms. In this study, we characterized the phyllosphere and rhizosphere microbiota of rice cultivars using a metaproteogenomic approach to get insight into the physiology of the bacteria and archaea that live in association with rice. The metaproteomic datasets gave rise to a total of about 4600 identified proteins and indicated the presence of one-carbon conversion processes in the rhizosphere as well as in the phyllosphere. Proteins involved in methanogenesis and methanotrophy were found in the rhizosphere, whereas methanol-based methylotrophy linked to the genus Methylobacterium dominated within the protein repertoire of the phyllosphere microbiota. Further, physiological traits of differential importance in phyllosphere versus rhizosphere bacteria included transport processes and stress responses, which were more conspicuous in the phyllosphere samples. In contrast, dinitrogenase reductase was exclusively identified in the rhizosphere, despite the presence of nifH genes also in diverse phyllosphere bacteria.

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“…The mxaF gene encodes the large subunit of the classical PQQ-linked methanol dehydrogenase, which catalyses the oxidation of methanol to formaldehyde in the majority of extant Gram-negative methylotrophic bacteria [23]. Using primers f1003 and r1561 and the protocol developed by McDonald and Murrell [24], we were able to amplify an approximately 340 bp mxaF gene fragment from DNA of strain Z T .…”

Section: Methylophilus Luteus Mim T (Fj872109)mentioning

confidence: 99%

Methylobacillus methanolivorans sp. nov., a novel non-pigmented obligately methylotrophic bacterium

Капаруллина

Trotsenko

Доронина

2017

International Journal of Systematic and Evolutionary Microbiology

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Three strains of obligately methylotrophic Betaproteobacteria (Z T , SP and M3) with the ribulose monophosphate pathway of C 1 assimilation are described. The isolates were strictly aerobic, Gram-stain-negative, asporogenous, motile (strains Z T and M3) or non-motile (strain SP) rods that multiplied by binary fisson, and were mesophilic and neutrophilic. All three strains utilized methanol but only strains SP and M3 utilized methylamine as carbon and energy sources. The prevailing cellular fatty acids were straight-chain saturated C 16 : 0 and unsaturated C 16 : 1 !7c acids. The major ubiquinone was Q-8. The predominant phospholipids were phosphatidylethanolamine, phosphatidylglycerol and cardiolipin. Ammonia was assimilated by glutamate dehydrogenase. The DNA G+C contents of strains Z T , SP and M3 were 51.0, 52.0 and 52.0 mol% (T m ), respectively. Levels of 16S rRNA gene sequence similarity between the three strains were very high (99.9-100 %), and they shared high levels of DNA-DNA relatedness (88-98 %). Based on 16S rRNA gene sequence analysis and DNA-DNA relatedness (19-30 %) with the type strains of the genus Methylobacillus, the novel isolates Z T , SP and M3 are classified as representing a novel species of this genus, for which the name Methylobacillus methanolivorans sp. nov. is proposed. The type strain is Z T (=VKM B-3037 T =JCM 31401 T =CCUG 68999 T ).Methylophilaceae, a family within the order Methylophilales, embraces the genera Methylophilus (type genus), Methylobacillus, Methylovorus and Methylotenera [1]. Betaproteobacterial obligate and restricted facultative methylotrophs are capable of utilizing methanol or methylamine as a sole source of carbon and energy via the ribulose monophosphate (RuMP) cycle. Because of similar morphology and metabolic organization, the main criteria used to clarify obligate methylobacteria into separate genera and species are their genomic and phylogenetic characteristics. On the other hand, members of the family are defined by some chemotaxonomic and biochemical properties, such as specific phospholipids and enzymes, which are used for the delineation of genera . In addition, another species of the genus, 'Methylobacillus rhizosphaerae', has not been validly published at the time of writing [7]. Here, we describe three novel betaproteobacterial methylotrophic strains, Z T , SP and M3, and show that they represent a novel species of the genus Methylobacillus.The novel strains were isolated from activated sludge of a drainage system of the Baikal paper mill (Irkutskaya oblast, Russia) (strain Z T ), from soil collected in St. Petersburg (Russia) (strain SP) and from municipal sewage water in Moscow (strain M3). All the strains were grown in liquid mineral medium 'K' containing (g l À1 ): KH 2 PO 4 -2.0; (NH 4 ) 2 SO 4 -2.0; MgSO 4 Á7H 2 O -0.025; NaCl -0.5; FeSO 4 Á7H 2 O -0.002, pH 7.2 and 0.5 % (v/v) CH 3 OH. The pH value was adjusted to 7.2 by adding 5 M NaOH. Solidified medium 'K' was prepared by adding 2.0 % (w/v) agar (Difco). The activated sludge (1 g...

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The structure and mechanism of methanol dehydrogenase

Cited by 140 publications

References 31 publications

Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase

Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase

Metaproteogenomic analysis of microbial communities in the phyllosphere and rhizosphere of rice

Methylobacillus methanolivorans sp. nov., a novel non-pigmented obligately methylotrophic bacterium

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