Photochemical cis-trans isomerisation of bovine rhodopsin at liquid helium temperatures

B. Aton, Robert Callender, B. Honig

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

RHODOPSIN is the visual pigment in the disk membranes of vertebrate rod photoreceptors. It consists of a chromophore, 11-cis-retinal, covalently bound in the form of a protonated Schiff base to an ε-amino group of a lysine in its apoprotein opsin. The primary photochemical event in visual excitation involves the formation of a species known as bathorhodopsin1 which has been detected at room temperature2 and at 4 K (ref. 3). The rhodopsin-bathorhodopsin transformation has been thought to involve a photochemical 11-cis → all-trans isomerisation; however, this conclusion has recently been questioned2-5 primarily because bathorhodopsin is formed within a few picoseconds at room temperature2 and in 36 ps at 4 K (ref. 3), and because of the large isotope effect involved in its formation3. In this letter, we show on the basis of resonance Raman experiments that isorhodopsin (the artificial pigment with 9-cis-retinal as its chromophore) is formed photochemically from rhodopsin at liquid helium temperatures. All models for the primary event other than isomerisation about the 11-12 double bond are found to be inconsistent with this result. We present a specific model (see also ref. 6) for the formation of bathorhodopsin which accounts for all the available data.

Original languageEnglish (US)
Pages (from-to)784-786
Number of pages3
JournalNature
Volume273
Issue number5665
DOIs
StatePublished - 1978
Externally publishedYes

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Helium
Rhodopsin
Temperature
Retinaldehyde
Opsins
Retinal Rod Photoreceptor Cells
Vertebrate Photoreceptor Cells
Apoproteins
Retinal Pigments
Schiff Bases
Isotopes
Lysine
Membranes
bathorhodopsin

ASJC Scopus subject areas

  • General

Cite this

Photochemical cis-trans isomerisation of bovine rhodopsin at liquid helium temperatures. / Aton, B.; Callender, Robert; Honig, B.

In: Nature, Vol. 273, No. 5665, 1978, p. 784-786.

Research output: Contribution to journalArticle

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