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Substrate binding to 15beta-hydroxylase (CYP106A2) probed by FT infrared spectroscopic studies of the iron ligand CO stretch vibration

Item Type:Article
Title:Substrate binding to 15beta-hydroxylase (CYP106A2) probed by FT infrared spectroscopic studies of the iron ligand CO stretch vibration
Creators Name:Simgen, B. and Contzen, J. and Schwarzer, R. and Bernhardt, R. and Jung, C.
Abstract:CYP106A2 has been expressed in E. coli with a high yield of up to 130 mg per litre of culture, purified to electrophoretic homogenity and found to be active in 15{beta}-hydroxylation of deoxycorticosterone using the adrenal redox proteins adrenodoxin and adrenodoxin reductase. Inspite of catalytic activity no substrate binding was detectable by UV-Vis spectroscopy. In contrast, an effect of substrate binding has been detected using the CO stretch mode infrared spectrum indicating that deoxycorticosterone binds in the heme pocket near the iron ligand.
Keywords:CYP106A2, Cytochrome P450(meg), Infrared Spectroscopy, Substrate Binding
Source:Biochemical and Biophysical Research Communications
ISSN:0006-291X
Publisher:Academic Press (U.S.A.)
Volume:269
Number:3
Page Range:737-742
Date:24 March 2000
Official Publication:https://doi.org/10.1006/bbrc.2000.2348
PubMed:View item in PubMed

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