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1h1o

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Revision as of 15:16, 29 October 2007 by OCA (Talk | contribs)
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Image:1h1o.gif

1h1o, resolution 2.13Å

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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

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