Fourier transform infrared study of the halorhodopsin chloride pump.
Fourier transform infrared study of the halorhodopsin chloride pump.
复制标题
氯化盐视紫红质泵的傅里叶变换红外研究。
DOI:
10.1021/bi00407a026
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发表时间:
1988
期刊:
影响因子:
2.9
通讯作者:
Spudich,JL
中科院分区:
文献类型:
--
作者:
Rothschild,KJ;Bousché,O;Braiman,MS;Hasselbacher,CA;Spudich,JL
Revised Manuscript Received January 19, 1988 abstract: Halorhodopsin (hR) is a light-driven chloride pump located in the cell membrane of Halo-bacterium halobium. Fourier transform infrared difference spectroscopy has been used to study structural alterations occurring during the hR photocycle. The frequencies of peaks attributed to the retinylidene chromophore are similar to those observed in the spectra of the related protein bacteriorhodopsin (bR), indicating that in hR as in bR an all-trans—13-ds isomerization occurs during formation of the early bathoproduct. Spectral featuresdue to protein structural alterations are also similar for the bR and hR photocycles. For example, formation of the red-shifted primary photoproducts of both hR and bR results in similar carboxyl peaks in the 1730-1745-cm" 1 region. However, in contrastto bR, no further changes are observed in the carboxyl region during subsequentsteps in the hR photocycle, indicating that additional carboxyl groups are not directly involved in chloride translocation. Overall, the close similarity of vibrations in hR and bR photoproduct difference spectra supports the existence of some common elements in the molecular mechanisms of energy transduction and active transport by these two proteins.Halorhodopsin (hR) 1 is a light-driven chloride pump found in the plasma membrane of Halobacterium halobium (Lanyi, 1986). In many respects, hR resembles the light-driven proton pump bacteriorhodopsin (bR) found in the purple membrane of the same organism. The two proteins have similar ab-