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

Research output: Contribution to journal › Article › peer-review

125 Scopus citations

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 - Jan 1 1978
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

Access to Document

10.1021/bi00605a028

Cite this

@article{f871eda6b7894b6191d5017097cb70b4,

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.",

author = "Doukas, {A. G.} and B. Aton and Callender, {R. H.} and Ebrey, {T. G.}",

year = "1978",

month = jan,

day = "1",

doi = "10.1021/bi00605a028",

language = "English (US)",

volume = "17",

pages = "2430--2435",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "12",

}

TY - JOUR

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 - 1978/1/1

Y1 - 1978/1/1

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.

UR - http://www.scopus.com/inward/record.url?scp=0017818529&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017818529&partnerID=8YFLogxK

U2 - 10.1021/bi00605a028

DO - 10.1021/bi00605a028

M3 - Article

C2 - 678522

AN - SCOPUS:0017818529

SN - 0006-2960

VL - 17

SP - 2430

EP - 2435

JO - Biochemistry

JF - Biochemistry

IS - 12

ER -

Resonance Raman Studies of Bovine Metarhodopsin I and Metarhodopsin II

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this