期刊
PHOTOCHEMISTRY AND PHOTOBIOLOGY
卷 85, 期 2, 页码 479-484出版社
WILEY
DOI: 10.1111/j.1751-1097.2008.00529.x
关键词
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For the first time to our knowledge, X-ray absorption spectroscopy (XAS) has been used to investigate the environment of putative Zn2+ binding sites in rhodopsin. We studied native purified nondeionized rhodopsin without any further addition of Zn2+, as well as with 1.5 mol of Zn2+-as zinc chloride-per mole of protein. Three different binding sites in rhodopsin were considered based on computational chemistry studies, and a quantitative analysis of the XAS signal was performed by fitting the experimental data to their simulated XAS spectra. Our results demonstrate that Zn2+ is intrinsically bound to rhodopsin and are compatible with the existence of an octahedral coordination involving six oxygen atoms in the first shell (average Zn-O distance of 2.08 angstrom), and with a second coordination shell containing one or two phosphorus or sulfur atoms at an average distance of 2.81 angstrom.
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