Protonation and deprotonation of the M, N, and O intermediates during the bacteriorhodopsin photocycle.
Protonation and deprotonation of the M, N, and O intermediates during the bacteriorhodopsin photocycle.
复制标题
细菌视紫红质光循环过程中 M、N 和 O 中间体的质子化和去质子化。
DOI:
10.1021/bi00481a015
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发表时间:
1990
期刊:
影响因子:
2.9
通讯作者:
Lanyi,JK
中科院分区:
文献类型:
--
作者:
Váró,G;Lanyi,JK
Department of Physiology and Biophysics, University of California, Irvine, California 92717 Received January 22, 1990; Revised Manuscript Received April 24, 1990 abstract: Transient pH changes were measured with phenol red and chlorophenol red in the 30^ s-50-ms time range during the photocycle of bacteriorhodopsin (BR), the light-driven proton pump. At pH> 7, the results confirmed earlier data and suggestions that one proton is released during the L-*·M reaction, and taken up again during the decay of N. These are likely to be steps in the proton transport process. At pH< 7, however, the time-resolved pH traces were complex and indicated additional protonation reactions. The data were explained by a model which assumed pH-dependent protonation states for M and N which varied from-1 to 0, and for O which varied from 0 to+ 2, relative to BR. If the kinetics of the vectorial proton translocation process were taken as pH independent, this treatment of the data suggested that a residue with a pMa of 5.9 was made protonable in M and N and two residues with pAla’s of 6.5 were made cooperatively protonable in O. The additional protons detected are not necessarily in the vectorial proton transfer pathway (ie, they are probably “Bohr protons”), and while theymust reflect conformational and/or neighboring ionization changes in theBR as it passes through the, N, and 0 states, their role, if any, in the transport is uncertain.