UNSPECIFIED (1999) Electron transfer reactions in the alkene mono-oxygenase complex from Nocardia corallina B-276. BIOCHEMICAL JOURNAL, 339 (Part 1). pp. 79-85. ISSN 0264-6021

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Abstract

Nocardia corallina B-276 possesses a multi-component enzyme, alkene mono-oxygenase (AMO), that catalyses the stereoselective epoxygenation of alkenes. The reductase component of this system has been shown by EPR and fluorescence spectroscopy to contain two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The role of these centres in the epoxygenation reaction was determined by midpoint potential measurements and electron transfer kinetics. The order of potentials of the prosthetic groups of the reductase were FAD/FAD(.) = -216mV, [2Fe-2S]/[2Fe-2S](.) = -160 mV and FAD(.)/FAD(..) = -134 mV. Combined, these data implied that the reductase component supplied the energy required for the epoxygenation reaction and allowed a prediction of the mechanism of electron transfer within the AMO complex. The FAD moiety was reduced by bound NADH in a two-electron reaction. The electrons were then transported to the [2Fe-2S] centre one at a time, which in turn reduced the di-iron centre of the epoxygenase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	BIOCHEMICAL JOURNAL
Publisher:	PORTLAND PRESS
ISSN:	0264-6021
Date:	1 April 1999
Volume:	339
Number:	Part 1
Number of Pages:	7
Page Range:	pp. 79-85
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/14636

Data sourced from Thomson Reuters' Web of Knowledge

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