遺伝子工学を用いたバクテリオロドプシンの構造と機能の解析

概要

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Molecular mechanism of light-driven proton pump by bacteriorhodopsin was studied by combinations of the site-directed mutagenesis and a varaiety of biochemical and biophysical methods. Using a synthetic bacterio-opsin gene in which 30 unique restriction sites are evenly spaced, we have carried out the extensive amino acid substitutions throughout the entire protein via the cassete mutagenesis. We concluded that Asp-85 and Asp-96 are involved in proton release and uptake step, respectively, and that charged residues including Asp-85, -212, Arg-82 around the protonated Schiff base are essential for determination of the purple color. And we postulated a tertiary structure model of bacteriorhodopsin.
日本生物物理学会の論文