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Effects of tyrosine-26 and tyrosine-64 nitration on the photoreactions of bacteriorhodopsinThe photoreactions of nitrated bacteriorhodopsin (bR) are examined. Flash-induced difference spectra of bR, bR with aminotyrosine in position 26 (bR-N26R) and bR with aminotyrosine in position 64 are analyzed. It is observed that changes in the actinic wavelength (from 520 to 500 or 580 nm) have no affect on the shape of the spectra and the formation and decay kinetics of the O and M intermediates. Nitration of tyrosine-64 decreases the chromophore absorbance, shifts the absorption maximum to 535 nm, and affects photocycle kinetics independent of the pK of its phenolic group. Light-dark adaptation spectra for bR are studied. The kinetics of the M and O intermediates in bR with nitrotyrosine in position 64 (bR-N64) and bR with aminotyrosine in position 64 and bR with nitrotyrosine in position 26 and bR-N26R are described and compared to bR; the pH dependence and M and O decay rates are considered. The deprotonation of bR-N64 during the photoreaction cycle and the effects of nitration on the activity of proton pumping are investigated.
Document ID
19860058697
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
Scherrer, P.
(California Univ. San Francisco, CA, United States)
Stoeckenius, W.
(California, University San Francisco, United States)
Date Acquired
August 12, 2013
Publication Date
January 1, 1985
Publication Information
Publication: Biochemistry
Volume: 24
Issue: 26 1
ISSN: 0006-2960
Subject Category
Chemistry And Materials (General)
Accession Number
86A43435
Funding Number(s)
CONTRACT_GRANT: NSG-7151
CONTRACT_GRANT: NIH-GM-27057
Distribution Limits
Public
Copyright
Other

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