The oxidation of methylamine in Paracoccus denitrificans

Authors :: A. H. Stouthamer
J.-W. L. De Gier
N. Harms
R. J. M. Van Spanning
J. van der Oost
Molecular Microbiology
Systems Bioinformatics
AIMMS
Source :: de Gier, J-W, van der Oost, J, Harms, N, Stouthamer, A H & Van Spanning, R J 1995, ' The oxidation of methylamine in Paracoccus denitrificans ', European Journal of Biochemistry, vol. 229, no. 1, pp. 148-54 . https://doi.org/10.1111/j.1432-1033.1995.0148l.x, European Journal of Biochemistry, 229(1), 148-54. Wiley-Blackwell
Publication Year :: 1995
Abstract: The in vivo oxidation of methylamine has been studied in Paracoccus denitrificans. Four components are involved in the electron transfer from methylamine to oxygen; methylamine dehydrogenase (MADH), amicyanin, cytochrome c and cytochrome-c oxidase. In P. denitrificans, MADH and its electron acceptor amicyanin are indispensable for growth on methylamine. In the present study, site-directed mutants have been used to demonstrate participation of cytochrome c550 and the aa3-type cytochrome-c oxidase. Moreover, evidence is provided for the operation of alternative routes, branching from amicyanin, in which at least cytochrome c1 and the cbb3-type cytochrome-c oxidase are involved.

Language :: English
ISSN :: 00142956
Database :: OpenAIRE
Journal :: de Gier, J-W, van der Oost, J, Harms, N, Stouthamer, A H & Van Spanning, R J 1995, ' The oxidation of methylamine in Paracoccus denitrificans ', European Journal of Biochemistry, vol. 229, no. 1, pp. 148-54 . https://doi.org/10.1111/j.1432-1033.1995.0148l.x, European Journal of Biochemistry, 229(1), 148-54. Wiley-Blackwell
Accession number :: edsair.doi.dedup.....b0389d418f37c4bc796cad11984476d0
Full Text :: https://doi.org/10.1111/j.1432-1033.1995.0148l.x