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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1978-10-18
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pubmed:abstractText |
The resonance Raman spectra of bovine metarhodopsin I and metarhodopsin II have been measured. The spectra are compared with model chromophore resonance Raman data. It was found that metarhodopsin I is linked to opsin via a protonated Schiff base linkage, whereas metarhodopsin II is linked by an unprotonated Schiff base. A recent suggestion that the chromophore of metarhodopsin II is retinal is explicitly disproved. The chromophores of both metarhodopsins are found to have an essentially all-trans conformation. The basic mechanism for color regulation in both forms appears to be electron delocalization. The data tend to support the model of cis-trans isomerization as the primary mechanism for vision. Also, the conclusions and inferences of this work on energy uses and storage by rhodopsin in neural generation are discussed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
17
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
2430-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:678522-Animals,
pubmed-meshheading:678522-Cattle,
pubmed-meshheading:678522-Energy Transfer,
pubmed-meshheading:678522-Photochemistry,
pubmed-meshheading:678522-Protein Conformation,
pubmed-meshheading:678522-Retinal Pigments,
pubmed-meshheading:678522-Rhodopsin,
pubmed-meshheading:678522-Schiff Bases,
pubmed-meshheading:678522-Spectrophotometry,
pubmed-meshheading:678522-Spectrum Analysis, Raman,
pubmed-meshheading:678522-Stereoisomerism
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pubmed:year |
1978
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pubmed:articleTitle |
Resonance Raman studies of bovine metarhodopsin I and metarhodopsin II.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|