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In vivo detection of a three iron cluster in fumarate reductase from Escherichia coli.

Abstract：

:Escherichia coli with plasmid amplified expression of fumarate reductase was grown anaerobically on a medium containing fumarate and glycerol and investigated by electron paramagnetic resonance spectroscopy. Anaerobically harvested cells exhibit an EPR signal characteristic of a reduced [2Fe-2S] cluster. Anaerobic addition of fumarate results in diminution of the reduced [2Fe-2S] signal and the appearance of the EPR signal associated with the oxidized 3Fe cluster. The results provide the first evidence for a trinuclear iron-sulfur cluster that exists in vivo, and suggest that the 3Fe cluster in purified fumarate reductase samples is not an artifact of the isolation procedure. The significance of this observation is discussed in relation to the physiological relevance of trinuclear iron-sulfur clusters.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Johnson MK,Morningstar JE,Cecchini G,Ackrell BA

doi

10.1016/0006-291x(85)91287-2

subject

Has Abstract

pub_date

1985-09-16 00:00:00

pages

653-8

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)91287-2

journal_volume

131

pub_type

杂志文章

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