Linked Life Data

7662871

Source:http://linkedlifedata.com/resource/pubmed/id/7662871

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1995-10-12
pubmed:abstractText
The hydrogen out-of-plane bending (HOOP) vibrations were studied in the difference Fourier transform infrared spectra of lumirhodopsin and metarhodopsin I by use of a series of specifically deuterated retinal derivatives of bovine rod outer segments. The 947 cm-1 band of lumirhodopsin and the 950 cm-1 band of metarhodopsin I were assigned to the mode composed of both 11-HOOP and 12-HOOP vibrations. This result suggests that the perturbation near C12-H of the retinal in the earlier intermediate, bathorhodopsin (Palings, van den Berg, Lugtenburg and Mathies, Biochemistry, 28 (1989) 1498-1507), is extinguished in lumirhodopsin and metarhodopsin I. Unphotolyzed rhodopsin and metarhodopsin I exhibited the 14-HOOP bands in the 12-D derivatives at 901 and 886 cm-1, respectively. Lumirhodopsin, however, did not show the 14-HOOP in the 12-D derivatives. The result suggests a change in geometrical alignment of the C14-H bond in lumirhodopsin with respect to the N-H bond of the Schiff base.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:articleTitle
Changes in structure of the chromophore in the photochemical process of bovine rhodopsin as revealed by FTIR spectroscopy for hydrogen out-of-plane vibrations.
pubmed:affiliation
Department of Biophysics, Faculty of Science, Kyoto University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't