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Mechanistic studies on methanol dehydrogenase

Antonie van Leeuwenhoek, 1985
Bacterial alcohol oxidation frequently proceeds via respiratory-chain linked dehydrogenases which have pyrrolo-quinoline quinone (PQQ) as their coenzyme. These so-called quinoprotein alcohol dehydrogenases have originally been isolated from methylotrophic bacteria and in these cases they are known as methanol dehydrogenases (EC 1.1.99.8).
M. Dijkstra, J. Frank Jzn, J. A. Duine
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Regulation of methanol dehydrogenase synthesis inParacoccus denitrificans

Antonie van Leeuwenhoek, 1989
The region downstream from the methanol dehydrogenase (MDH) structural gene has been cloned and sequenced. MDH promoter activity have been studied by using a broad-host-range promoter probe vector.
Harms, N   +3 more
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The structure and mechanism of methanol dehydrogenase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
This is a review of recent work on methanol dehydrogenase (MDH), a pyrroloquinoline quinone (PQQ)-containing enzyme catalysing the oxidation of methanol to formaldehyde in methylotrophic bacteria. Although it is the most extensively studied of this class of dehydrogenases, it is only recently that there has been any consensus about its mechanism.
Christopher, Anthony, Paul, Williams
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Methanol dehydrogenase structure

1996
Methanol dehydrogenase (MEDH, EC 1.1.99.8) is a soluble quinoprotein located in the periplasmic space of many methylotrophic bacteria (Anthony, 1986). The enzyme catalyzes the oxidation of methanol to formaldehyde, utilizing the single carbon compound as the sole source of carbon and energy.
Z.-X. Xia   +6 more
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Demonstration of methanol dehydrogenase in methanol assimilating yeasts

Experientia, 1975
Eine induzierbare Methanoldehydrogenase wurde in Zellextrakten von 2 Methanol assimilierenden Hefen,Pichia pinus undKloeckera sp. 2201, festgestellt, die entweder von NAD oder DCPIP abhangig waren. Nicotinamid Adenin-Dinukleotidphosphat diente jedoch nicht als Elektronen-Akzeptor.
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The biochemistry of methanol dehydrogenase

1996
Methanol dehydrogenase (MDH) is responsible for oxidation of methanol to formaldehyde in almost all bacteria growing aerobically on methane or methanol; it is a periplasmic quinoprotein which passes its electrons to a specific c-type cytochrome which is usually called cytochrome c L (Anthony, 1986, 1992, 1993, Goodwin and Anthony, 1995).
Christopher Anthony, Simon L. Dales
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Amperometric detection of methanol with a methanol dehydrogenase modified electrode sensor

Journal of Electroanalytical Chemistry, 2007
Abstract An amperometric enzyme electrode was developed by immobilizing the quinoprotein methanol dehydrogenase from Methylobacterium extorquens AM1 onto a glassy carbon electrode. Ferrocene (FC), ferrocene carboxylic acid, N , N , N ′, N ′-tetramethyl-1,4-phenylenediamine (TMPD), N , N -dimethyl- p -phenylenediamine (DMPD), phenazine ...
Qinfeng Liu, Jon R. Kirchhoff
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Methanol Dehydrogenase, a PQQ-Containing Quinoprotein Dehydrogenase

2000
Methanol dehydrogenase (MDH; EC 1.1.99.8) catalyses the oxidation of methanol to formaldehyde in the periplasm of methylotrophic bacteria during growth on methanol or methane. It was first described in Methylobacterium extorquens (Anthony and Zatman, 1964a,b) and has subsequently been shown to be the one feature that is common to almost all ...
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The quinoprotein dehydrogenases for methanol and glucose

Archives of Biochemistry and Biophysics, 2004
This review summarises our current understanding of two of the main types of quinoprotein dehydrogenase in which pyrroloquinoline quinone (PQQ) is the only prosthetic group. These are the soluble methanol dehydrogenase and the membrane glucose dehydrogenase (mGDH).
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Formaldehyde dehydrogenase preparations from Methylococcus capsulatus (Bath) comprise methanol dehydrogenase and methylene tetrahydromethanopterin dehydrogenase

Microbiology, 2004
In methylotrophic bacteria, formaldehyde is an important but potentially toxic metabolic intermediate that can be assimilated into biomass or oxidized to yield energy. Previously reported was the purification of an NAD(P)(+)-dependent formaldehyde dehydrogenase (FDH) from the obligate methane-oxidizing methylotroph Methylococcus capsulatus (Bath ...
Ekundayo K, Adeosun   +5 more
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