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2bt6

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[[Category: transit peptide]]
[[Category: transit peptide]]
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Revision as of 14:42, 30 October 2007

Image:2bt6.gif

2bt6, resolution 1.50Å

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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 ... [(full description)]

About this Structure

2BT6 is a [Single protein] structure of sequence from [Bos taurus] with MG, FES and RUA as [ligands]. Structure known Active Site: AC1. 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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