1h1o
From Proteopedia
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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 ... [(full description)]
About this Structure
1H1O is a [Single protein] structure of sequence from [Acidithiobacillus ferrooxidans] with SO4, ZN, HEM and GOL as [ligands]. 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 Mon Oct 29 17:21:03 2007
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