The oxidation of methylamine in Paracoccus denitrificans

J.-W. de Gier; J. van der Oost; N Harms; A.H. Stouthamer; R J Van Spanning

doi:10.1111/j.1432-1033.1995.0148l.x

The oxidation of methylamine in Paracoccus denitrificans

J.-W. de Gier, J. van der Oost, N Harms, A.H. Stouthamer, R J Van Spanning

AIMMS

Research output: Contribution to Journal › Article › Academic › peer-review

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.

Original language	English
Pages (from-to)	148-54
Number of pages	7
Journal	European Journal of Biochemistry
Volume	229
Issue number	1
DOIs	https://doi.org/10.1111/j.1432-1033.1995.0148l.x
Publication status	Published - 1 Apr 1995

Keywords

Methylamines
Mutagenesis, Site-Directed
Oxidation-Reduction
Paracoccus denitrificans
Journal Article
Research Support, Non-U.S. Gov't

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1111/j.1432-1033.1995.0148l.x

Persistent URL (handle)

Persistent link

Cite this

@article{8d22ad0732cc4eabbbf4ac2a10ff0495,

title = "The oxidation of methylamine in Paracoccus denitrificans",

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.",

keywords = "Methylamines, Mutagenesis, Site-Directed, Oxidation-Reduction, Paracoccus denitrificans, Journal Article, Research Support, Non-U.S. Gov't",

author = "{de Gier}, J.-W. and {van der Oost}, J. and N Harms and A.H. Stouthamer and {Van Spanning}, {R J}",

year = "1995",

month = apr,

day = "1",

doi = "10.1111/j.1432-1033.1995.0148l.x",

language = "English",

volume = "229",

pages = "148--54",

journal = "European Journal of Biochemistry",

issn = "0014-2956",

publisher = "Wiley-Blackwell Publishing Ltd",

number = "1",

}

TY - JOUR

T1 - The oxidation of methylamine in Paracoccus denitrificans

AU - de Gier, J.-W.

AU - van der Oost, J.

AU - Harms, N

AU - Stouthamer, A.H.

AU - Van Spanning, R J

PY - 1995/4/1

Y1 - 1995/4/1

N2 - 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.

AB - 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.

KW - Methylamines

KW - Mutagenesis, Site-Directed

KW - Oxidation-Reduction

KW - Paracoccus denitrificans

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1111/j.1432-1033.1995.0148l.x

DO - 10.1111/j.1432-1033.1995.0148l.x

M3 - Article

C2 - 7744026

SN - 0014-2956

VL - 229

SP - 148

EP - 154

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

IS - 1

ER -

The oxidation of methylamine in Paracoccus denitrificans

Abstract

Keywords

UN SDGs

Access to Document

Persistent URL (handle)

Fingerprint

Cite this