Incorporation of 19F‐substituted aromatic amino acids into membrane proteins from chromatophores of Rhodospirillum rubrum G9+

FEBS Letters

Bachofen, R.¹  Ghosh, R.²  Hauser, H.² 

[1] Institut für Pflanzenbiologie und Mikrobiologie, Zollikerstr. 107, CH-8008, Zürich, Switzerland;Laboratorium für Biochemie, Universitätsstr. 16, ETH-Zentrum, CH-8092 Zürich, Switzerland

关键词: 19F-NMR;    Membrane protein;    Membrane dynamics;    Chromatophore membrane;    Light-harvesting complex;    Protein modification;   

DOI  :  10.1016/0014-5793(85)80884-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Chromatophore membranes were isolated from cells of the carotenoidless mutant Rhodospirillum rubrum G9⁺ grown in the presence of several fluorinated aromatic amino acids, solubilized using SDS and the extent of incorporation analyzed using high-resolution ¹⁹F-NMR spectroscopy. 3- and 4-¹⁹F-phenylalanine, 6-¹⁹F-tryptophan and 3-¹⁹F-tyrosine were biosynthetically incorporated into membrane proteins whereas 5-¹⁹F-tryptophan and 2-¹⁹F-phenylalanine were inhibitors of cell growth. The polypeptide chains of the major chromatophore membrane protein the light-harvesting complex, were isolated and shown by high-resolution ¹⁹F-NMR to contain 3-¹⁹F-phenylalanine, which is known to be situated principally within the membrane hydrocarbon layer. Broad-band ¹⁹F-NMR spectra of 3-¹⁹F-phenylalanine-labelled chromatophores showed the phenyl ring to be immobilized within the membrane.

【 授权许可】

Unknown