FEBS Letters | |
Transmembrane orientation of α‐helices and the organization of chlorophylls in photosynthetic pigment‐protein complexes | |
Nabedryk, Eliane1  Breton, Jacques1  | |
[1] Service de Biophysique, Département de Biologie, CEN Saclay, 91191 Gif-sur- Yvette, Cêdex, France | |
关键词: Chlorophyll-protein complex; α-Helix; β-Sheet; UV circular dichroism; Infrared dichroism; Transmembrane orientation; CD; circular dichroism; IR; infrared; Chl; chlorophyll; BChl; bacteriochlorophyll; LHC; lightharvesting complex; | |
DOI : 10.1016/0014-5793(84)81196-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
UV CD and IR spectra of the water-soluble bacteriochlorophyll-protein antenna isolated from Prosthecochloris aestuarii indicate that about 50% of the protein is in a β-sheet conformation while for the dominant antenna complexes isolated from bacteria (B800-850) and from green plants (LHC), the α-helix (45%) is more abundant than the β-sheet (~ 10%) conformation. Furthermore, IR dichroism studies show that the α-helical segments of a large variety of intrinsic membrane Chl-protein complexes (antenna and reaction centers) are tilted on the average at 30–35° away from the membrane normal. The observation that in these complexes the Chl planes are also tilted at about the same angle suggests that the transmembrane orientation of the α-helices determines the positioning of the Chl molecules in photosynthetic membranes.
【 授权许可】
Unknown
【 预 览 】
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