title: [Effects of ultraviolet-B radiation on protein structure in PS II using Fourier transform infrared spectroscopy].
abstract: The effects of ultraviolet-B (UV-B) radiation on protein structure in photosystem II (PS II) was studied using Fourier transform infrared spectroscopy. The results demonstrated that irradiation of the plant with enhanced UV-B caused the change in the structures of protein in PSII. The intensity of alpha-helix, beta-sheet was increased, while the intensity of beta-turn was decreased. The coupling of those structures with surrounding became weaker with UV-B radiation. Otherwise, the UV-B influenced the structure of tyrosine residue and made the polarity of tyrosine decrease. The changes caused by UV-B radiation could alter the combination between Mn cluster and pigments with protein inevitably. It would lead to a series of changes, such as the process of light transmission and conversion, electron transfer and oxygen evolution.
authors.affiliation: Key Laboratory of Resource Biology and Biotechnology in Western China, Ministry of Education, Northwest University, Xi'an 710069, China. liuxiao@nwu.edu.cn
authors.forename: Xiao
authors.initials: X
authors.lastname: Liu
authors.forename: Weng-Ting
authors.initials: WT
authors.lastname: Tang
authors.forename: Qian
authors.initials: Q
authors.lastname: Li
authors.forename: Ming
authors.initials: M
authors.lastname: Yue
mesh_terms: D045332:Photosystem II Protein Complex / Q000737:chemistry* / Q000528:radiation effects; D017550:Spectroscopy, Fourier Transform Infrared; D014466:Ultraviolet Rays
chemical_list: D045332:Photosystem II Protein Complex