A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of photosystem II by FTIR spectroscopy

FEBS Letters

Carpentier, R.¹  Ahmed, A.¹  Tajmir-Riahi, H.A.¹ 

[1] Centre de recherche en photobiophysique, Université du Québec a Trois-Rivières, CP. 500, Trois-Rivières, Québec, G9A 5H7, Canada

关键词: 33 kDa extrinsic;    Protein;    Conformation;    PSII reaction center;    FTIR spectroscopy;    PSII;    photosystem II;    SDS;    sodium dodecyl sulfate;    CD;    circular dichroism;    FTIR;    Fourier transform infrared;   

DOI  :  10.1016/0014-5793(95)00282-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In chloroplast photosystem II, the extrinsic polypeptide of 33 kDa is involved in the stabilization the Mn cluster in charge of water splitting and in the fulfillment of the Ca²⁺-cofactor requirement for oxygen evolution. The conformational analysis of the purified 33 kDa extrinsic polypeptide was carried out using FTIR spectroscopy with its self-deconvolution and second derivative resolution enhancement as well as curve-fitting procedures. The FTIR spectroscopic results showed that the isolated polypeptide is characterized by a major proportion β-sheet conformation (36%) with 27% α-helix, 24% turn, and 13% β-antiparallel structures.

【 授权许可】

Unknown