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Time-resolved resonance Raman characterization of the bO/sub 640/ intermediate of bacteriorhodopsin. Reprotonation of the Schiff base

Journal Article · · Biochemistry; (United States)
OSTI ID:5424055
; ; ;
The resonance Raman spectrum of photolyzed bacteriorhodopsin under conditions known to increase the concentration of the bO/sub 640/ intermediate in both H/sub 2/O and D/sub 2/O is presented. By use of computer subtraction techniques and a knowledge of the Raman spectra of the unphotolyzed bacteriorhodopsin as well as the other intermediates in the cycle, a qualitative spectrum of bO/sub 640/ is determined. The shift of a band at 1630 cm/sup -1/ in H/sub 2/O to 1616 cm/sup -1/ in D/sub 2/O suggests that the Schiff base of bO/sub 640/ is protonated. Additional bands at 947, 965, and 992 cm/sup -1/ that appear only in D/sub 2/O suspensions confirm that a proton is coupled to the retinal chromophore of bO/sub 640/. The reprotonation of the Schiff base thus occurs during the bM/sub 412/ to bO/sub 640/ step. The fingerprint region, sensitive to the isomeric configuration of the retinal chromophore of bO/sub 640/, is dissimilar to the fingerprint regions of published model compounds and other forms of bacteriorhodopsin.
Research Organization:
Univ. of California, Los Angeles
OSTI ID:
5424055
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 18:16; ISSN BICHA
Country of Publication:
United States
Language:
English

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Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BARYONS
CHARGED-PARTICLE TRANSPORT
CHEMICAL REACTIONS
DECOMPOSITION
ELEMENTARY PARTICLES
FERMIONS
HADRONS
HEAVY WATER
HYDROGEN COMPOUNDS
IMINES
NUCLEONS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXYGEN COMPOUNDS
PHOTOCHEMICAL REACTIONS
PHOTOLYSIS
PIGMENTS
PROTON TRANSPORT
PROTONS
RADIATION TRANSPORT
RAMAN SPECTRA
REACTION INTERMEDIATES
RESOLUTION
SCHIFF BASES
SPECTRA
TIME RESOLUTION
TIMING PROPERTIES
WATER