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Structure and Function of Retinochrome
Author(s) -
Tokunaga Fumio,
Yoshihara Kazuo
Publication year - 1995
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.199500036
Subject(s) - chemistry , rhodopsin , ring (chemistry) , counterion , cyclohexene , stereochemistry , membrane , isomerase , crystallography , retinal , biochemistry , ion , enzyme , organic chemistry , catalysis
Retinochrome is a photo‐isomerase of all‐ trans ‐retinal to the 11‐ cis ‐isomer for rhodopsin synthesis. This protein is probably folded into seven α‐helices spanning the membranes. Upon irradiation, it is converted to metaretinochrome, via pre‐lumi‐ and lumiretinochrome, which are stable under 50 and 250 K, respectively. A series of analogue studies revealed that the cyclohexene ring and 6‐ s‐cis ‐twisted conformation are important for binding. Modification of the 14‐position suggests close location of the 14‐H to the counterion.