西亚试剂：Identification of a single peridinin sensing Chl-a excitati

发布时间：2025-10-14

Identification of a single peridinin sensing Chl-a excitation in reconstituted PCP by crystallography and spectroscopy

Tim Schultea,1, Dariusz M. Niedzwiedzkib,1,2, Robert R. Birgeb, Roger G. Hillerc, Tomá? Polívkad,e, Eckhard Hofmanna,3 and Harry A. Frankb,3

aBiophysics, Department of Biology and Biotechnology, Ruhr-University Bochum, D-44780 Bochum, Germany;
bDepartment of Chemistry, University of Connecticut, Storrs, CT 06269-3060;
cBiology Department, Faculty of Science, Macquarie University, NSW 2109, Australia;
dInstitute of Physical Biology, University of South Bohemia, 373-33 Nove Hrady, Czech Republic; and
eBiological Centre, Czech Academy of Sciences, Ceske Budejovice, Czech Republic

The peridinin-chlorophyll a-protein (PCP) of dinoflagellates is unique among the large variety of natural photosynthetic light-harvesting systems. In contrast to other chlorophyll protein complexes, the soluble PCP is located in the thylakoid lumen, and the carotenoid pigments outnumber the chlorophylls. The structure of the PCP complex consists of two symmetric domains, each with a central chlorophyll a (Chl-a) surrounded by four peridinin molecules. The protein provides distinctive surroundings for the pigment molecules, and in PCP, the specific environment around each peridinin results in overlapping spectral line shapes, suggestive of different functions within the protein. One particular Per, Per-614, is hypothesized to show the strongest electronic interaction with the central Chl-a. We have performed an in vitro reconstitution of pigments into recombinant PCP apo-protein (RFPCP) and into a mutated protein with an altered environment near Per-614. Steady-state and transient optical spectroscopic experiments comparing the RFPCP complex with the reconstituted mutant protein identify specific amino acid-induced spectral shifts. The spectroscopic assignments are reinforced by a determination of the structures of both RFPCP and the mutant by x-ray crystallography to a resolution better than 1.5 ?. RFPCP and mutated RFPCP are unique in representing crystal structures of in vitro reconstituted light-harvesting pigment-protein complexes.

• 以上资料由西亚试剂：http://www.xiyashiji.com/ 提供此产品的详细信息如密度,含量,分子式,分子量等均可在西亚官网查询   
• 相关产品如溴化汞硝酸亚汞氯化亚汞乙酸苯汞氯化钾汞 碘化汞钾硫氰酸汞硫酸亚汞氧化汞氯化汞碘化汞硝酸汞三氯氧磷三氯化磷碘甲烷二碘甲烷三碘甲烷三氟碘甲烷氘代碘甲烷碘乙烷1,2-二碘乙烷甲酸铷碘化铷溴化铷铬酸铷硫酸铷氟化铷硝酸铷氯化铷碳酸铷硫酸镱 碳酸镱氯化镱硝酸镱氧化镱等均有销售.欢迎订购

上一篇：“大科学”模式有助于提速生命科学研究？
下一篇：苏利股份拟对百力化学增资