Results 201 to 210 of about 107,783 (244)

Methanol Dehydrogenase: Mechanism of Action

Antonie van Leeuwenhoek, 1989
Methanol dehydrogenase (MDH, EC 1.1.99.8) was first described in 1964 by Anthony and Zatman (Anthony and Zatman 1964, 1965, 1967a,b). Since that time a large number of MDH’s have been found with similar properties (Anthony 1986) including the dimeric MDH from Hyphomicrobium X (Duine et al. 1978).
Frank, J., Dijkstra, M., Balny, C., Verwiel, P.E.J., Duine, J.A.   +4 more
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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, van Spanning, R J, Oltmann, L F, Stouthamer, A.H.   +3 more
openaire   +2 more sources

Electrochemical conversion of carbon dioxide to methanol with the assistance of formate dehydrogenase and methanol dehydrogenase as biocatalysts

Journal of the American Chemical Society, 1994
Electrolysis at potentials between -0.7 and -0.9 V vs SCE of carbon dioxide-saturated phosphate buffer solutions (pH7) containing formate dehydrogenase (FDH) and either methyl viologen (MV[sup 2+]) or pyrroloquinolinequinone (PQQ) as an electron mediator yielded formate with current efficiencies as high as 90%.
Susumu Kuwabata, Ryo Tsuda, Hiroshi Yoneyama   +2 more
openaire   +1 more source

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.
openaire   +2 more sources

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
openaire   +1 more source

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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In Silico Studies of the Mechanism of Methanol Oxidation by Quinoprotein Methanol Dehydrogenase

Journal of the American Chemical Society, 2003
The mechanism of bacterial methanol dehydrogenase involves hydride equivalent transfer from substrate to the ortho-quinone PQQ to provide a C5-reduced intermediate that subsequently rearranges to the hydroquinone PQQH(2). We have studied the PQQ reduction by molecular dynamic (MD) simulations in aqueous solution.
Swarnalatha Y, Reddy, Thomas C, Bruice
openaire   +2 more sources

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
openaire   +1 more source

Effects of Ca2+ on the Activity and Stability of Methanol Dehydrogenase

Journal of Protein Chemistry, 2000
The effects of exogenously added Ca2+ on the enzymatic activity and structural stability of methanol dehydrogenase were studied for various Ca2+ concentrations. Methanol dehydrogenase activity increased significantly with increasing concentration of Ca2+, approaching saturation at 200 mM Ca2+.
Y, Zhao, G, Wang, Z, Cao, Y, Wang, H, Cheng, H M, Zhou   +5 more
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Characterization of the substrate scope of an alcohol dehydrogenase commonly used as methanol dehydrogenase

Bioorganic & Medicinal Chemistry Letters, 2019
Many alcohol dehydrogenases (ADHs) catalyze oxidation of a broad scope of alcohols. When an NAD-dependent ADH oxidizes methanol, albeit at a poor rate, it may be treated as methanol dehydrogenase (MDH). One ADH from Geobacillus stearothermophilus DSM 2334 (GsADH) has been widely used as MDH, but its actual substrate scope remains less characterized ...
Xiaojia, Guo, Yanbin, Feng, Xueying, Wang, Yuxue, Liu, Wujun, Liu, Qing, Li, Junting, Wang, Song, Xue, Zongbao K, Zhao   +8 more
openaire   +2 more sources