Open AccessThe Oxidation of Methylamine in Paracoccus denitrificans
Author(s) -
Gier JanWillem L.,
Oost John,
Harms Nellie,
Stouthamer Adriaan H.,
Spanning Rob J. M.
Publication year - 1995
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1995.0148l.x
Subject(s) - paracoccus denitrificans , methylamine , cytochrome c oxidase , cytochrome , cytochrome b , cytochrome c , chemistry , biochemistry , cytochrome c1 , coenzyme q – cytochrome c reductase , enzyme , mitochondrion , mitochondrial dna , gene
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 c 550 and the aa 3 ‐type cytochrome‐ c oxidase. Moreover, evidence is provided for the operation of alternative routes, branching from amicyanin, in which at least cytochrome c 1 and the cbb 3 ‐type cytochrome‐ c oxidase are involved.