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  • Title: The oxidation of methylamine in Paracoccus denitrificans.
    Author: De Gier JW, Van der Oost J, Harms N, Stouthamer AH, Van Spanning RJ.
    Journal: Eur J Biochem; 1995 Apr 01; 229(1):148-54. PubMed ID: 7744026.
    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.
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