Three-dimensional model of zeaxanthin binding PsbS protein associated with nonphotochemical quenching of excess quanta of light energy absorbed by the photosynthetic apparatus |
| |
Authors: | Prafulla K Haripal Hemant K Raval Mukesh K Raval Rakesh M Rawal Basanti Biswal Udaya C Biswal |
| |
Institution: | (1) P.G. Department of Chemistry, Government College, Sundargarh, Orissa, 770002, India;(2) Welspun India Ltd., Welspun City, Anjar, Gujarat, 370110, India;(3) Biochemistry Laboratory, Gujarat Cancer and Research Institute, Ahmedabad, Gujarat, 380001, India;(4) School of Life Sciences, Sambalpur University, Jyoti Vihar, Orissa, 768019, India |
| |
Abstract: | A three-dimensional model of the PsbS protein was built with the help of homology-modeling methods. This protein is also known as CP22 and is associated with the protection of photosystem II of thylakoid from excess quanta of light energy absorbed by the photosynthetic apparatus. PsbS is reported to bind two molecules of zeaxanthin at low pH (<5.0) and is believed to be essential for rapid nonphotochemical quenching (qE) of chlorophyll a fluorescence in photosystem II. An attempt was made to explain the pH modulation of the conformation of protein through salt-bridges Glu−(122)-Lys+(113) and Glu−(226)-Lys+(217). Binding of two molecules of zeaxanthin in the three-dimensional model of PsbS is postulated. The molecular mechanism of photoprotection by PsbS is explained through the model.
1 Backbone structure of the PsbS protein with two molecules of all trans zeaxanthin (ZEX). Residues Glu 90, 122, 194, 226 and Lys 113, 217 are shown. The figure is drawn with RASMOL (Molecular Visualization Program, RasMol V2.6, Roger Sayle, Glaxo Wellcome Research and Development, Stevenage, Hertfordshire, UK)
Electronic Supplementary Material Supplementary material is available for this article at |
| |
Keywords: | PsbS protein Homology modeling Photoprotection Nonphotochemical quenching Zeaxanthin Photosystem II |
本文献已被 PubMed SpringerLink 等数据库收录! |
|