1h1o
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The study of electron transfer between the copper protein rusticyanin | + | The study of electron transfer between the copper protein rusticyanin (RCy) and the c(4)-cytochrome CYC(41) of the acidophilic bacterium Acidithiobacillus ferrooxidans has evidenced a remarkable decrease of RCy's redox potential upon complex formation. The structure of the CYC(41) obtained at 2.2 A resolution highlighted a specific glutamate residue (E121) involved in zinc binding as potentially playing a central role in this effect, required for the electron transfer to occur. EPR and stopped-flow experiments confirmed the strong inhibitory effect of divalent cations on CYC(41):RCy complex formation. A docking analysis of the CYC(41) and RCy structure allows us to propose a detailed model for the complex-induced tuning of electron transfer in agreement with our experimental data, which could be representative of other copper proteins involved in electron transfer. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Abergel, C.]] | [[Category: Abergel, C.]] | ||
[[Category: Bruschi, M.]] | [[Category: Bruschi, M.]] | ||
| - | [[Category: Claverie, J | + | [[Category: Claverie, J M.]] |
| - | [[Category: Guidici-Orticoni, M | + | [[Category: Guidici-Orticoni, M T.]] |
[[Category: Malarte, G.]] | [[Category: Malarte, G.]] | ||
[[Category: Nitschke, W.]] | [[Category: Nitschke, W.]] | ||
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[[Category: heme]] | [[Category: heme]] | ||
| - | ''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 12:56:24 2008'' |
Revision as of 10:56, 21 February 2008
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ACIDITHIOBACILLUS FERROOXIDANS CYTOCHROME C4 STRUCTURE SUPPORTS A COMPLEX-INDUCED TUNING OF ELECTRON TRANSFER
Overview
The study of electron transfer between the copper protein rusticyanin (RCy) and the c(4)-cytochrome CYC(41) of the acidophilic bacterium Acidithiobacillus ferrooxidans has evidenced a remarkable decrease of RCy's redox potential upon complex formation. The structure of the CYC(41) obtained at 2.2 A resolution highlighted a specific glutamate residue (E121) involved in zinc binding as potentially playing a central role in this effect, required for the electron transfer to occur. EPR and stopped-flow experiments confirmed the strong inhibitory effect of divalent cations on CYC(41):RCy complex formation. A docking analysis of the CYC(41) and RCy structure allows us to propose a detailed model for the complex-induced tuning of electron transfer in agreement with our experimental data, which could be representative of other copper proteins involved in electron transfer.
About this Structure
1H1O is a Single protein structure of sequence from Acidithiobacillus ferrooxidans with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The structure of Acidithiobacillus ferrooxidans c(4)-cytochrome: a model for complex-induced electron transfer tuning., Abergel C, Nitschke W, Malarte G, Bruschi M, Claverie JM, Giudici-Orticoni MT, Structure. 2003 May;11(5):547-55. PMID:12737820
Page seeded by OCA on Thu Feb 21 12:56:24 2008
Categories: Acidithiobacillus ferrooxidans | Single protein | Abergel, C. | Bruschi, M. | Claverie, J M. | Guidici-Orticoni, M T. | Malarte, G. | Nitschke, W. | GOL | HEM | SO4 | ZN | C4 | Cytochrome | Electron transfer | Heme
