The methylamine oxidizing system of Pseudomonas AM1 reconstituted with purified components.

Abstract:

:The electron transport system coupled to the oxidation of methylamine in Pseudomonas AM1 was investigated by reconstituting it from the highly purified components. A mixture of methylamine dehydrogenase, cytochrome cH and cytochrome c oxidase (= cytochrome aa3) actively oxidized methylamine (161 mol of O2 consumed/mol of heme a of cytochrome c oxidase X min). In this system, addition of amicyanin did not affect the oxygen consumption rate. The oxygen consumption rate of the cell-free extract prepared from the cells cultivated in a copper-deficient medium was directly proportional to the amount of amicyanin added, and extrapolation to zero copper concentration gave a value of 28 mol of O2 consumed/mol of heme a of cytochrome c oxidase X min. These results suggest that methylamine oxidation in the bacterium can occur at least to some extent without participation of amicyanin.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Fukumori Y,Yamanaka T

doi

10.1093/oxfordjournals.jbchem.a121929

subject

Has Abstract

pub_date

1987-02-01 00:00:00

pages

441-5

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

101

pub_type

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