Resonance Raman studies of bovine metarhodopsin I and metarhodopsin II
- 13 June 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 17 (12) , 2430-2435
- https://doi.org/10.1021/bi00605a028
Abstract
The resonance Raman spectra of bovine metarhodopsin I and metarhodopsin II were measured. The spectra were compared with model chromophore resonance Raman data. Metarhodopsin I was linked to opsin via a protonated Schiff base linkage; metarhodopsin II was linked by an unprotonated Schiff base. A recent suggestion that the chromophore of metarhodopsin II is retinal was explicitly disproved. The chromophores of both metarhodopsins had an essentially all-trans conformation. The basic mechanism for color regulation in both forms appeared to be electron delocalization. The data tended to support the model of cis-trans isomerization as the primary mechanism for vision. The conclusions and inferences of this work on energy uses and storage by rhodopsin in neural generation were discussed.This publication has 7 references indexed in Scilit:
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