TAILIEUCHUNG - Báo cáo khoa học: Dynamics in electron transfer protein complexes

Electron transfer proteins transport electrons safely between large redox enzymes. The complexes formed by these proteins are among the most transient. The biological function requires, on the one hand, sufficient spec-ificity of the interaction to allow for rapid and selective electron transfer, and, on the other hand, a fast turnover of the complex. | IFEBS Journal MINIREVIEW Dynamics in electron transfer protein complexes Qamar Bashir Sandra Scanu and Marcellus Ubbink Leiden Institute of Chemistry Leiden University Gorlaeus Laboratories The Netherlands Keywords cytochrome encounter complex NMR plastocyanin transient complex Correspondence M. Ubbink Leiden Institute of Chemistry Leiden University Gorlaeus Laboratories . Box 9502 2300 RA Leiden The Netherlands Fax 31 71527 5856 Tel 31 7152 74628 E-mail Received 23 November 2010 revised 8 February 2011 accepted 22 February 2011 doi Electron transfer proteins transport electrons safely between large redox enzymes. The complexes formed by these proteins are among the most transient. The biological function requires on the one hand sufficient specificity of the interaction to allow for rapid and selective electron transfer and on the other hand a fast turnover of the complex. Recent progress in the characterization of the nature of these complexes has demonstrated that the encounter state plays an important role. This state of initial binding is dominated by electrostatic interactions and consists of an ensemble of orientations. Paramagnetic relaxation enhancement NMR and chemical shift perturbation analysis provide ways for the experimental characterisation of the encounter state. Several studies that have used these techniques have shown that the surface area sample in the encounter state can be limited to the immediate environment of the final specific complex. The encounter complex can represent a large fraction and in some small complexes no specific binding is detected at all. It can be concluded that in electron transfer protein complexes a fine balance is sought between the low-specificity encounter state and the high-specificity productive complex to meet the opposing requirements of rapid electron transfer and a high turnover rate. Introduction Protein-protein interactions form the basis of .

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