Electron transfer reactions in the alkene mono-oxygenase complex from Nocardia corallina B-276
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 0264-6021Full text not available from this repository.
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|
|Date:||1 April 1999|
|Number of Pages:||7|
|Page Range:||pp. 79-85|
Actions (login required)