Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1997-3-20
pubmed:abstractText
The effects of ionic strength on formation and decay of metarhodopsin II (MII), the active photointermediate of bovine rhodopsin, were studied in the native membrane environment by means of ultraviolet/ visible and Fourier-transform infrared (FTIR) spectroscopy. By increasing the concentration of KCl in the range from hypotonic to 4 M, the apparent pKa of the metarhodopsin I(MI)/MII equilibrium is shifted by approximately pH three, in favor of the MII intermediate. In addition, the apparent rate of MII formation is enhanced by an increase in ionic strength (about twofold in the presence of 2 M KCl). MIII decay is independent of the salt concentration. Attenuated-total-reflectance/FTIR data show that the high-salt conditions have no effect on the rigidity of the membrane matrix and do not induce structural changes in the intermediates themselves. Different salts were tested for their ability to shift the MI/MII equilibrium; however, no clear ion dependence was observed. We interpret these results as an indication for direct involvement of the cytosolic surface charge in the regulation of the photochemical activity of bovine rhodopsin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
243
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
174-80
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Modulation of the metarhodopsin I/metarhodopsin II equilibrium of bovine rhodopsin by ionic strength--evidence for a surface-charge effect.
pubmed:affiliation
Department of Biochemistry F.M.W., Institute of Cellular Signalling, University of Nijmegen, The Netherlands. frankl@sci.kun.nl
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't