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Paracoccus denitrificans dehydrogenase

Harms, N. Reijnders, W.N. Anazawa, H. van der Palen, C.J. van Spanning, R.J. Oltmann, L.E Stouthamer, A.H. Identification of a two-compo-nent regulatory system controlling methanol dehydrogenase synthesis in Paracoccus denitrificans. Mol. Microbiol., 8, 457-470 (1993)... [Pg.466]

Alefounder, P. R., and Ferguson, S. J., 1981, A periplasmic location for methanol dehydrogenase from Paracoccus denitrificans implications for proton pumping by cytochrome aa3. Biochem. Biophys. Res. Comm. 98 778n784. [Pg.112]

Harris, T. K., and Davidson, V. L., 1993a, A new kinetic model for the steady-state reactions of the quinoprotein methanol dehydrogenase from Paracoccus-denitrificans. Biochemistry 32 4362n4368. [Pg.115]

Long, A. R., and Anthony, C., 1991, The periplasmic modifier protein for methanol dehydrogenase in the methylotrophs Methylophilus methylotrophus and Paracoccus denitrificans. Journal of General Microbiology 137 235392360. [Pg.116]

Gray, K. A., Davidson, V. L., and Knaff, D. B., 1988, Complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificans, J. Biol. Chem. 263 13987n 13990. [Pg.142]

Amicyanin is found in methylotrophic bacteria that can use methylated amines as an energy source. The inactivation of the amicyanin gene in Paracoccus denitrificans results in complete loss of its ability to grow on methylamine, a direct indication that amicyanin is a key component of the methylamine driven electron-transfer chain. Amicyanin accepts an electron from methylamine dehydrogenase and transfers it to a c-type cytochrome (see Section 5.4.5). Currently, more than a dozen amicyanin and pseudoazurin sequences are available. [Pg.1019]

Pathways can yield reliable predictions of the electronic couplings, where the CT process in proteins are mediated by the interactions of a single or multiple configurations that the protein can adopt [50]. Pathways has been successfully applied to a number of CT processes in protein environment. For instance, the electron transfer between the proteins cytochrome c2 (cytc2) and the photosynthetic reaction center (RC) [152] in order to determine the protein structural dependence of this CT reaction, also, to look at the impact of structural and conformational variations on the electronic coupling between the proteins methylamine dehydrogenase and amicyanin from Paracoccus denitrificans [153]. [Pg.121]

Xia ZX, Dai WW, He YN, White SA, Mathews FS, Davidson VL (2003) X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome C-551L J Biol Inotg Chem 8 843-854... [Pg.258]


See other pages where Paracoccus denitrificans dehydrogenase is mentioned: [Pg.26]    [Pg.95]    [Pg.140]    [Pg.149]    [Pg.688]    [Pg.352]    [Pg.472]    [Pg.235]    [Pg.318]    [Pg.70]    [Pg.114]    [Pg.253]    [Pg.178]    [Pg.252]    [Pg.1025]    [Pg.112]    [Pg.91]   


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Paracoccus denitrificans

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