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The oxidation of methylamine in <em>Paracoccus denitrificans</em>.

Authors :
De Gier, Jan-Willem L.
Van Der Oost, John
Harms, Nellie
Stouthamer, Adriaan H.
Van Spanning, Rob J.M.
Source :
European Journal of Biochemistry. 4/1/95, Vol. 229 Issue 1, p148-154. 7p.
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 eytochrome-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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
229
Issue :
1
Database :
Academic Search Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
12900950
Full Text :
https://doi.org/10.1111/j.1432-1033.1995.0148l.x