Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans
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منابع مشابه
Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans.
Methylamine dehydrogenase from Paracoccus denitrificans was purified to homogeneity in two steps from the periplasmic fraction of methylamine-grown cells. The enzyme exhibited a pI value of 4.3 and was composed of two 46,700-dalton subunits and two 15,500-dalton subunits. Each small subunit possessed a covalently bound pyrrolo-quinoline quinone prosthetic group. The amino acid compositions of t...
متن کاملSteady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans.
A steady-state kinetic analysis was performed of the reaction of methylamine and phenazine ethosulphate (PES) with the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans. Experiments with methylamine and PES as varied-concentration substrates produced a series of parallel reciprocal plots, and when the concentrations of these substrates were varied in a constant ratio a linear...
متن کاملAn inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role.
When grown on methylamine as a sole carbon source, Paracoccus denitrificans synthesizes a Type I blue copper protein which mediates electron transfer between methylamine dehydrogenase and cytochrome c. This blue copper protein does not serve as an electron acceptor for methanol dehydrogenase and is not synthesized by cells grown on methanol or succinate. The blue copper protein and methylamine ...
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In [ l ] low concentrations of Tinopal AN, (1,l-bis(3,N-5-dimethylbenzoxazol-2-y1)methine p-toluene sulphonate), which is present in the optical brightener Uvitex AN (Ciba-Geigy Ltd) [2], inhibited the aerobic respiration of Paracoccus denitrificans. Using inverted membrane vesicles of P. denitrifcans [I], this inhibition was shown to occur in the NADH dehydrogenase (EC 1.66.99.3) region of the...
متن کاملPurification, characterization and crystallization of the F-ATPase from Paracoccus denitrificans
The structures of F-ATPases have been determined predominantly with mitochondrial enzymes, but hitherto no F-ATPase has been crystallized intact. A high-resolution model of the bovine enzyme built up from separate sub-structures determined by X-ray crystallography contains about 85% of the entire complex, but it lacks a crucial region that provides a transmembrane proton pathway involved in the...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1987
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.169.4.1712-1717.1987