Results 241 to 250 of about 108,904 (277)

Nicotinoprotein methanol dehydrogenase enzymes in Gram-positive methylotrophic bacteria

Journal of Molecular Catalysis B: Enzymatic, 2000
A novel type of alcohol dehydrogenase enzyme has been characterized from Gram-positive methylotrophic (Bacillus methanolicus, the actinomycetes Amycolatopsis methanolica and Mycobacterium gastri) and non-methylotrophic bacteria (Rhodococcus strains). Its
Lubbert Dijkhuizen
exaly   +2 more sources

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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
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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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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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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
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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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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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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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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, W.-W. Dai, Y. N. He, S. A. White, G. D. Boyd, F. S. Mathews, V. L. Davidson   +6 more
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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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