| pubmed-article:2790007 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2790007 | lifeskim:mentions | umls-concept:C0035499 | lld:lifeskim |
| pubmed-article:2790007 | lifeskim:mentions | umls-concept:C0034107 | lld:lifeskim |
| pubmed-article:2790007 | lifeskim:mentions | umls-concept:C0549255 | lld:lifeskim |
| pubmed-article:2790007 | lifeskim:mentions | umls-concept:C0023089 | lld:lifeskim |
| pubmed-article:2790007 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:2790007 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:2790007 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
| pubmed-article:2790007 | lifeskim:mentions | umls-concept:C2347517 | lld:lifeskim |
| pubmed-article:2790007 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:2790007 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:2790007 | pubmed:dateCreated | 1989-11-22 | lld:pubmed |
| pubmed-article:2790007 | pubmed:abstractText | Primary photochemical behaviors of cattle rhodopsin analogues (Rh5 and Rh7) having cyclopenta- and cycloheptatrienylidene 11-cis-locked retinals (Ret5 and Ret7, respectively) were studied by excitation with a picosecond laser pulse (wavelength 532 nm; duration 21 ps). Picosecond absorption and fluorescence measurements of Rh5 showed formation of only a long-lived excited singlet state (tau l/e = 85 ps). The excited state of the retinal analogue having a five-membered ring was stabilized in protein (Rh5) more than in solvent (protonated Schiff base of Ret5; PSB5). Excitation of Rh7 produced two ground-state photoproducts, Rh7 (580) and Rh7 (630). According to the analysis of photon density dependency, Rh7 (580) was a single-photon product of Rh7, while Rh7 (630) was the photoproduct of Rh7 (580). Fluorescence emitted from a seven-membered ring system like Rh7 or a protonated Schiff base of Ret7 (PSB7) was weaker than that in a corresponding five-membered ring system, especially in protein (Rh7). The difference in photoreaction between Rh5 and Rh7 may originate from the difference in fixation of the 11-cis form. On the basis of the spectral and kinetic similarities between Rh7 (580) and photorhodopsin, a precursor of bathorhodopsin, it was proposed that both have twisted all-trans chromophores in the way of the isomerization. The protein moiety of rhodopsin which fixes the chromophore at both ends seems to accelerate the rotation of the C11-C12 double bond and to prevent it from going through relaxation processes other than the isomerization. This may be a plausible reason why rhodopsin has a large quantum yield (0.67). | lld:pubmed |
| pubmed-article:2790007 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2790007 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2790007 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2790007 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2790007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2790007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2790007 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2790007 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:2790007 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2790007 | pubmed:author | pubmed-author:ItoMM | lld:pubmed |
| pubmed-article:2790007 | pubmed:author | pubmed-author:NakanishiKK | lld:pubmed |
| pubmed-article:2790007 | pubmed:author | pubmed-author:TsukidaKK | lld:pubmed |
| pubmed-article:2790007 | pubmed:author | pubmed-author:YoshizawaTT | lld:pubmed |
| pubmed-article:2790007 | pubmed:author | pubmed-author:ShichidaYY | lld:pubmed |
| pubmed-article:2790007 | pubmed:author | pubmed-author:Balogh-NairVV | lld:pubmed |
| pubmed-article:2790007 | pubmed:author | pubmed-author:MatuokaSS | lld:pubmed |
| pubmed-article:2790007 | pubmed:author | pubmed-author:KandoriHH | lld:pubmed |
| pubmed-article:2790007 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2790007 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:2790007 | pubmed:volume | 28 | lld:pubmed |
| pubmed-article:2790007 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2790007 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2790007 | pubmed:pagination | 6460-7 | lld:pubmed |
| pubmed-article:2790007 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:meshHeading | pubmed-meshheading:2790007-... | lld:pubmed |
| pubmed-article:2790007 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2790007 | pubmed:articleTitle | Mechanism of isomerization of rhodopsin studied by use of 11-cis-locked rhodopsin analogues excited with a picosecond laser pulse. | lld:pubmed |
| pubmed-article:2790007 | pubmed:affiliation | Department of Biophysics, Faculty of Science, Kyoto University, Japan. | lld:pubmed |
| pubmed-article:2790007 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2790007 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2790007 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2790007 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2790007 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2790007 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2790007 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2790007 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2790007 | lld:pubmed |
