2bt6

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spinqualitylabelsall models 2bt6, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

RU(BPY)2(MBPY)-MODIFIED BOVINE ADRENODOXIN

Overview

Bovine adrenodoxin (Adx) plays an important role in the electron-transfer, process in the mitochondrial steroid hydroxylase system of the bovine, adrenal cortex. Using electron paramagnetic resonance (EPR) spectroscopy, we showed that photoreduction of the [2Fe-2S] cluster of Adx via, (4'-methyl-2,2'-bipyridine)bis(2,2'-bipyridine)ruthenium(II), [Ru(bpy)2(mbpy)] covalently attached to the protein surface can be used as, a new approach to probe the "shuttle" hypothesis for the electron transfer, by Adx. The 1.5 A resolution crystal structure of a 1:1, Ru(bpy)2(mbpy)-Adx(1-108) complex reveals the site of modification, Cys95, and allows to predict the possible intramolecular electron-transfer, pathways within the complex. Photoreduction of uncoupled Adx, mutant, Adx(1-108), and Ru(bpy)2(mbpy)-Adx(1-108) using safranin T as the, mediating electron donor suggests that two electrons are transferred from, the dye to Adx. The intramolecular photoreduction rate constant for the, ruthenated Adx has been determined and is discussed according to the, predicted pathways.

About this Structure

2BT6 is a Single protein structure of sequence from Bos taurus with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Light-induced reduction of bovine adrenodoxin via the covalently bound ruthenium(II) bipyridyl complex: intramolecular electron transfer and crystal structure., Halavaty A, Muller JJ, Contzen J, Jung C, Hannemann F, Bernhardt R, Galander M, Lendzian F, Heinemann U, Biochemistry. 2006 Jan 24;45(3):709-18. PMID:16411746

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