In vivo studies of primary alcohols, aldehydes and carboxylic acids as electron donors for the methane mono-oxygenase in a variety of methanotrophs

D. J. Leak, H. Dalton

Research output: Contribution to journalArticle

Abstract

C2 to C4 primary alcohols and their corresponding aldehydes were oxidized by type I, type II and type X obligate methanotrophs. Reducing equivalents from each oxidation step could be utilized, in vivo, to stimulate methane mono-oxygenase activity. As neither oxidation step produces NADH directly, these observations are presented as evidence for reverse electron transport in methanotrophs. In type II methanotrophs, 5 mM-acetate, propionate and butyrate also stimulate methane mono-oxygenase activity apparently by inducing the breakdown of poly-β-hydroxybutyrate, subsequent metabolism of β-hydroxybutyrate giving rise to NADH.

Original languageEnglish
Pages (from-to)3487-3497
Number of pages11
JournalJournal of General Microbiology
Volume129
Issue number11
Publication statusPublished - 1 Jan 1983

ASJC Scopus subject areas

  • Microbiology

Cite this

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abstract = "C2 to C4 primary alcohols and their corresponding aldehydes were oxidized by type I, type II and type X obligate methanotrophs. Reducing equivalents from each oxidation step could be utilized, in vivo, to stimulate methane mono-oxygenase activity. As neither oxidation step produces NADH directly, these observations are presented as evidence for reverse electron transport in methanotrophs. In type II methanotrophs, 5 mM-acetate, propionate and butyrate also stimulate methane mono-oxygenase activity apparently by inducing the breakdown of poly-β-hydroxybutyrate, subsequent metabolism of β-hydroxybutyrate giving rise to NADH.",
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T1 - In vivo studies of primary alcohols, aldehydes and carboxylic acids as electron donors for the methane mono-oxygenase in a variety of methanotrophs

AU - Leak, D. J.

AU - Dalton, H.

PY - 1983/1/1

Y1 - 1983/1/1

N2 - C2 to C4 primary alcohols and their corresponding aldehydes were oxidized by type I, type II and type X obligate methanotrophs. Reducing equivalents from each oxidation step could be utilized, in vivo, to stimulate methane mono-oxygenase activity. As neither oxidation step produces NADH directly, these observations are presented as evidence for reverse electron transport in methanotrophs. In type II methanotrophs, 5 mM-acetate, propionate and butyrate also stimulate methane mono-oxygenase activity apparently by inducing the breakdown of poly-β-hydroxybutyrate, subsequent metabolism of β-hydroxybutyrate giving rise to NADH.

AB - C2 to C4 primary alcohols and their corresponding aldehydes were oxidized by type I, type II and type X obligate methanotrophs. Reducing equivalents from each oxidation step could be utilized, in vivo, to stimulate methane mono-oxygenase activity. As neither oxidation step produces NADH directly, these observations are presented as evidence for reverse electron transport in methanotrophs. In type II methanotrophs, 5 mM-acetate, propionate and butyrate also stimulate methane mono-oxygenase activity apparently by inducing the breakdown of poly-β-hydroxybutyrate, subsequent metabolism of β-hydroxybutyrate giving rise to NADH.

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M3 - Article

VL - 129

SP - 3487

EP - 3497

JO - Journal of General Microbiology

JF - Journal of General Microbiology

SN - 0022-1287

IS - 11

ER -