Effect of changing the position and orientation of Asp85 relative to the protonated Schiff base within the retinal cavity on the rate of photoisomerization in bacteriorhodopsin

Journal Article · Thu Jun 13 00:00:00 EDT 1996 · Journal of Physical Chemistry

DOI:https://doi.org/10.1021/jp960734r· OSTI ID:375677

Song, L; El-Sayed, M A ^[1]; Lanyi, J K ^[2]

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1. Georgia Inst. of Technology, Atlanta, GA (United States)
2. Univ. of California, Irvine, CA (United States)

Replacement of either Val49 with Ala or Ala53 with Val by site-specific mutagenesis is known to change the position and orientation of the protonated Schiff base relative to Asp85 within the retinal cavity of bacteriorhodopsin (bR). The effect of mutation on the rate of the subpicosecond photoisomerization of retinal in bR is examined by using a pump-probe technique. A decrease in the rate of photoisomerization of retinal in V49A and A53V is observed. This is discussed in terms of the previously proposed mechanism of the protein catalysis of retinal photoisomerization process in bR. 17 refs., 2 figs., 1 tab.

• DOE Contract Number: FG03-88ER13828
• OSTI ID: 375677
• Journal Information: Journal of Physical Chemistry, Journal Name: Journal of Physical Chemistry Journal Issue: 24 Vol. 100; ISSN JPCHAX; ISSN 0022-3654
• Country of Publication: United States
• Language: English

Related Subjects

40 CHEMISTRY
55 BIOLOGY AND MEDICINE
BASIC STUDIES
ABSORPTION SPECTRA
BACTERIA
EXCITED STATES
ISOMERIZATION
MOLECULAR STRUCTURE
PHOTOCHEMICAL REACTIONS
PROTEINS
RHODOPSIN
SCHIFF BASES