Resonance Raman Studies of Bovine Metarhodopsin I and Metarhodopsin II

A. G. Doukas; B. Aton; R. H. Callender; T. G. Ebrey

doi:10.1021/bi00605a028

Resonance Raman Studies of Bovine Metarhodopsin I and Metarhodopsin II

A. G. Doukas, B. Aton, R. H. Callender, T. G. Ebrey

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Abstract

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 derealization. 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.

Original language	English (US)
Pages (from-to)	2430-2435
Number of pages	6
Journal	Biochemistry
Volume	17
Issue number	12
DOIs	https://doi.org/10.1021/bi00605a028
State	Published - 1978
Externally published	Yes

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Biochemistry

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title = "Resonance Raman Studies of Bovine Metarhodopsin I and Metarhodopsin II",

abstract = "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 derealization. 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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year = "1978",

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journal = "Biochemistry",

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publisher = "American Chemical Society",

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T1 - Resonance Raman Studies of Bovine Metarhodopsin I and Metarhodopsin II

AU - Doukas, A. G.

AU - Aton, B.

AU - Callender, R. H.

AU - Ebrey, T. G.

PY - 1978

Y1 - 1978

N2 - 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 derealization. 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.

AB - 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 derealization. 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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Resonance Raman Studies of Bovine Metarhodopsin I and Metarhodopsin II

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