2bt6
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Bovine adrenodoxin (Adx) plays an important role in the electron-transfer | + | 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== | ==About this Structure== | ||
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[[Category: Jung, C.]] | [[Category: Jung, C.]] | ||
[[Category: Lendzian, F.]] | [[Category: Lendzian, F.]] | ||
| - | [[Category: Mueller, J | + | [[Category: Mueller, J J.]] |
[[Category: FES]] | [[Category: FES]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:25 2008'' |
Revision as of 14:41, 21 February 2008
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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 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
Page seeded by OCA on Thu Feb 21 16:41:25 2008
Categories: Bos taurus | Single protein | Bernhardt, R. | Contzen, J. | Galander, M. | Halavaty, A. | Hannemann, F. | Heinemann, U. | Jung, C. | Lendzian, F. | Mueller, J J. | FES | MG | RUA | 2fe-2s | Bovine adrenodoxin | Electron transport | Intramolecular electron transfer | Iron | Iron-sulfur | Metal-binding | Mitochondrion | Ruthenium(ii) bipyridyl complex | Transit peptide
