Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Dehydrogenases quinoprotein dehydrogenase

Conversion of methanol into formaldehyde by methanol dehydrogenase. A complex array of genes is involved in this oxidation and the dehydrogenase contains pyrroloquinoline quinone (PQQ) as a cofactor (references in Ramamoorthi and Lidstrom 1995). Details of its function must, however, differ from that of methylamine dehydrogenase that also contains a quinoprotein—tryptophan tryptophylquinone (TTQ). [Pg.297]

Anthony C (1992) The structure of bacterial quinoprotein dehydrogenases. Int J Biochem 24 29-39. [Pg.324]

A recently characterized class of dehydrogenases are the quinoproteins which contain a pyrroloquinolene quinone prosthetic group and do not require a separate co-factor Electron transfer mediators such as phenazine ethosulphate 2,6-dichloroindophenol and ferricenium ions have been used to recycle the quinoprotein the reduce mediator is detected amperometrically. [Pg.66]

Davis G, Hill HAG, Aston WJ, Higgins IJ, Turner APR 1983. Bioelectrochemical fuel cell and sensor based on a quinoprotein, alcohol dehydrogenase. Enzyme Microb Technol 5 383-388. [Pg.631]

E. D Costa, J. Higgins, and A.P. Turner, Quinoprotein glucose dehydrogenase and its application in an amperometric glucose sensor. Biosensors 2, 71—87 (1986). [Pg.91]

M. Yamada, M. Elias, K. Matsushita, C.T. Migita, and O. Adachi, Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase its structure comparison with other quinoproteins. Biochim. Biophys. Acta Proteins Proteomics 1647, 185-192 (2003). [Pg.600]

C. Anthony, M. Ghosh, and C.C. Blake, The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone. Biochem. J. 304, 665-674 (1994). [Pg.600]

B. Groen, J. Frank Jr, and J.A. Duine, Quinoprotein alcohol dehydrogenase from ethanol-grown Pseudomonas aeruginosa. Biochem. J. 223, 921-924 (1984). [Pg.600]

One-electron reduction of PQQ gives rise to formation of the semiquinone, PQQH whereas two-electron reduction leads to formation of the quinol form, PQQH2 (Figure 2). Both species have been implicated as occurring in the redox reactions catalyzed by quinoprotein dehydrogenases, since electron transfer to the respiratory chain occurs in one-electron steps [12],... [Pg.566]

Table 2 Absorption Maxima of Quinoprotein Dehydrogenase Forms and Model Complexes... Table 2 Absorption Maxima of Quinoprotein Dehydrogenase Forms and Model Complexes...
Quinoprotein dehydrogenases containing PQQ or TTQ have been shown to function in various microorganisms in addition to the NAD(P)-dependent and flavo-protein dehydrogenases. The PQQ-containing dehydrogenases require Ca (or Mg) for structural as well as catalytic purposes. However, the mechanism of activation of PQQ, the substrate or the hemiketal adduct by the metal ion, is still unknown. [Pg.580]

Cozier, G. E., and Anthony, C. (1995a). Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobact-erium extorquens. Biochem. J., 312, 679-685. [Pg.69]

Ghosh, M., Anthony, C., Harlos, K., Goodwin, M. G., and Blake, C. (1995). The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium ex-torquens at 1.94 A. Structure, 3, 177-187. [Pg.70]

J. Frebortova, K. Matsushita, H. Arata, and O. Adachi, Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus a redox-titration study, Biochim. Biophys. Acta 1363, 24-34 (1998). [Pg.263]

Flavin oxidases include d- and l-amino acid oxidases, and some amine oxidases, although others are quinoproteins (Section 9.8.3). In these enzymes, the flavin is reduced by dehydrogenation of the substrate, byway of an intermediate substrate-flavin adduct, as occurs in the dehydrogenases (Section 7.3.3). [Pg.186]

Methanol Dehydrogenase, a PQQ-Contauiing Quinoprotein Dehydrc enase... [Pg.105]

The c-type cytochromes of methylotrophic bacteria. Biochim. Biophys. The structure of hacterial quinoprotein dehydrogenases, Int. J. Biochem. [Pg.113]

Anthony, C., 1993a, Methanol dehydrogenase in Gram-negative bacteria. In Principles and applications of quinoproteins, (V. L. Davidson, ed.), Marcel Dekker, New York, pp. 17945. [Pg.113]

Anthony, C., and Ghosh, M., 1998, The structure and function of the PQQ-containing quinoprotein dehydrogenases. Progress in Biophysics and Molecular Biology 69 1921. [Pg.113]


See other pages where Dehydrogenases quinoprotein dehydrogenase is mentioned: [Pg.132]    [Pg.311]    [Pg.600]    [Pg.113]    [Pg.614]    [Pg.161]    [Pg.207]    [Pg.127]    [Pg.22]    [Pg.568]    [Pg.568]    [Pg.572]    [Pg.574]    [Pg.576]    [Pg.361]    [Pg.312]    [Pg.437]    [Pg.73]    [Pg.74]    [Pg.74]    [Pg.75]    [Pg.79]    [Pg.85]    [Pg.85]    [Pg.93]    [Pg.97]    [Pg.103]    [Pg.106]    [Pg.107]    [Pg.109]   
See also in sourсe #XX -- [ Pg.1146 ]




SEARCH



Quinoprotein dehydrogenase

Quinoprotein dehydrogenase electrode

Quinoprotein dehydrogenase electrode wired

Quinoprotein glucose dehydrogenase

Wired quinoprotein dehydrogenase

© 2024 chempedia.info