2bt6: Difference between revisions
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==Overview== | ==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 .. | 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== | ||
2BT6 is a | 2BT6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, FES and RUA as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BT6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
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Revision as of 16:21, 5 November 2007
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RU(BPY)2(MBPY)-MODIFIED BOVINE ADRENODOXIN
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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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- 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