Light- and dark-adapted bacteriorhodopsin, a time-resolved neutron diffraction study.
Light- and dark-adapted bacteriorhodopsin, a time-resolved neutron diffraction study.
复制标题
光适应和暗适应的细菌视紫红质,一种时间分辨中子衍射研究。
DOI:
10.1016/0005-2736(90)90331-h
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发表时间:
1990
期刊:
影响因子:
--
通讯作者:
G. Büldt
中科院分区:
文献类型:
--
作者:
N. Dencher;G. Papadopoulos;D. Dresselhaus;G. Büldt
Recently, neutron diffraction experiments have revealed well-resolved and reversible changes in the protein conformation of bacteriorhodopsin (BR) between the light-adapted ground state and the M-intermediate of the proton pumping photocycle (Dencher, Dresselhaus, Zaccai and Büldt (1989) Proc. Natl. Acad. Sci. USA 86, 7876–7879). These changes are triggered by the light-induced isomerization of the chromophore retinal from the all-trans to the 13-cis configuration. Dark-adapted purple membranes contain a mixture of two pigment species with either the all-trans- or 13-cis-retinal isomer as chromophore. Employing a time-resolved neutron diffraction technique, no changes in protein conformation in the resolution regime of up to 7 Å are observed during the transition between the two ground-state species 13-cis-BR and all-trans-BR. This is in line with the fact that the conversion of all-trans BR to 13-cis-BR involves an additional isomerization about the C15 N Schiff's base bond, which in contrast to M formation minimizes retinal displacement and keeps the Schiff's base in the original protein environment. Furthermore, there is no indication for large-scale redistribution of water molecules in the purple membrane during light-dark adaptation.
影响因子:
2.9
作者:
P. Scherrer;M. Mathew;W. Sperling;W. Stoeckenius
通讯作者:
P. Scherrer;M. Mathew;W. Sperling;W. Stoeckenius
影响因子:
3.4
作者:
M. Tsuda;T. Ebrey
通讯作者:
M. Tsuda;T. Ebrey