Linked Life Data

11384968

Source:http://linkedlifedata.com/resource/pubmed/id/11384968

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2001-8-6
pubmed:abstractText
Absorption of light in rhodopsin leads through 11-cis- and all-trans-retinal isomerization, proton transfers, and structural changes to the active G-protein binding meta-II state. When meta-II is photolysed by blue light absorption, the activating pathway is apparently reverted, and rhodopsin is photoregenerated. However, the product formed, a P subspecies with A(max) = 500 nm (P(500)), is different from the ground state based on the following observations: (i) the ground state fingerprint of 11-cis-retinal does not appear in the infrared spectra, although the proton transfers and structural changes are reverted; (ii) extraction of the retinal from P(500) does not yield the expected stoichiometric amount of 11-cis-retinal but predominantly yields all-trans-retinal; (iii) the infrared spectrum of P(500) is similar to the classical meta-III intermediate, which arises from meta-II by thermal decay; and (iv) both P(500) and meta-III can be photoconverted to meta-II with the same changes in the infrared spectrum and without a significant change in the isomerization state of the extracted chromophore. The data indicate the presence of a "second switch" between active and inactive conformations that operates by photolysis but without isomerization around the C(11)-C(12) double bond. This emphasizes the exclusivity of the ground state, which is only accessible by the metabolic regeneration with 11-cis-retinal.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30161-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Signaling states of rhodopsin: absorption of light in active metarhodopsin II generates an all-trans-retinal bound inactive state.
pubmed:affiliation
Institute for Medical Physics and Biophysics, Medizinische Fakultät Charité, Humboldt University, Schumann Strasse 20-21, 10098 Berlin, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't