The interaction domain of the redox protein adrenodoxin is mandatory for binding of the electron acceptor CYP11A1, but is not required for binding of the electron donor adrenodoxin reductase

Item Type:	Article
Title:	The interaction domain of the redox protein adrenodoxin is mandatory for binding of the electron acceptor CYP11A1, but is not required for binding of the electron donor adrenodoxin reductase
Creators Name:	Heinz, A. and Hannemann, F. and Mueller, J.J. and Heinemann, U. and Bernhardt, R.
Abstract:	Adrenodoxin (Adx) is a [2Fe-2S] ferredoxin involved in electron transfer reactions in the steroid hormone biosynthesis of mammals. In this study, we deleted the sequence coding for the complete interaction domain in the Adx cDNA. The expressed recombinant protein consists of the amino acids 1-60, followed by the residues 89-128, and represents only the core domain of Adx (Adx-cd) but still incorporates the [2Fe-2S] cluster. Adx-cd accepts electrons from its natural redox partner, adrenodoxin reductase (AdR), and forms an individual complex with this NADPH-dependent flavoprotein. In contrast, formation of a complex with the natural electron acceptor, CYP11A1, as well as electron transfer to this steroid hydroxylase is prevented. By an electrostatic and van der Waals energy minimization procedure, complexes between AdR and Adx-cd have been proposed which have binding areas different from the native complex. Electron transport remains possible, despite longer electron transfer pathways. © 2005 Elsevier Inc. All rights reserved.
Keywords:	Adrenodoxin, CYP11A1, Electron transfer, Electrostatic potential, Ferredoxin-NADP+ reductase, Protein-protein interaction, Animals, Cattle
Source:	Biochemical and Biophysical Research Communications
ISSN:	0006-291X
Publisher:	Academic Press
Volume:	338
Number:	9
Page Range:	491-498
Date:	29 August 2005
Official Publication:	https://doi.org/10.1016/j.bbrc.2005.08.077
PubMed:	View item in PubMed

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