The role of the non-covalent β-ionone-ring binding site in rhodopsin: historical and physiological perspective-Reference-Cited by-同舟云学术

The role of the non-covalent β-ionone-ring binding site in rhodopsin: historical and physiological perspective

Published:2015 Issue:11 Volume:14 Page:1932-1940
ISSN:1474-905X
Container-title:Photochemical & Photobiological Sciences
language:en
Short-container-title:Photochem. Photobiol. Sci.

Author:

Matsumoto Hiroyuki¹²³⁴⁵,Iwasa Tatsuo⁶⁷⁸⁹,Yoshizawa Tôru¹⁰¹¹¹²⁹

Affiliation:

1. Department of Biochemistry and Molecular Biology

2. University of Oklahoma Health Sciences Center

3. Oklahoma City

4. USA

5. Clinical Proteomics and Gene Therapy Laboratory

6. Muroran Institute of Technology

7. Graduate School of Engineering

8. Hokkaido 050-8585

9. Japan

10. Department of Biophysics

11. Kyoto University

12. Kyoto 606-8502

Abstract

Rhodopsin regenerates by way of a non-covalent complex formation between the 11-cis retinal and opsin, rendering the β-ionone ring-binding pocket a distinct physiological role.

Funder

National Eye Institute

Publisher

Springer Science and Business Media LLC

Subject

Physical and Theoretical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/PP/C5PP00158G

Reference50 articles.

1. Existence of a β-ionone ring-binding site in the rhodopsin molecule

2. On the Mechanism of Schiff Base Formation and Hydrolysis

3. THE DARK ADAPTATION OF RETINAL FIELDS OF DIFFERENT SIZE AND LOCATION

4. Molecular Genetics of Human Color Vision: The Genes Encoding Blue, Green, and Red Pigments

5. Primary structures of chicken cone visual pigments: vertebrate rhodopsins have evolved out of cone visual pigments.

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