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PMID: 6303466 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Activation of phosphodiesterase by rhodopsin and its analogues.

Biophysics of structure and mechanism ·Vol. 9 ·No. 4 ·1983-00-00 ·Pages 245-58

Yoshizawa T, Fukada Y

Abstract

Activation of guanosine 3',5'-cyclic monophosphate (cGMP) phosphodiesterase (EC 3.1.4.35.) in frog rod outer segment membrane by rhodopsin and its analogues was investigated. The Schiff-base linkage between opsin and retinal in rhodopsin was not always necessary for the phosphodiesterase activation. The binding of beta-ionone ring of retinal to a hydrophobic region of opsin was not enough to induce the enzyme activation. A striking photo-activation of the enzyme was induced by photo-isomerization of rhodopsin analogues from cis to trans form. It seems probable that an "expanded" conformation of opsin around the retinylidene chromophore induced by the cis to trans isomerization may be the trigger for the activation of phosphodiesterase. On the other hand, the phosphodiesterase in frog rod outer segment was activated by warming of bathorhodopsin to -12 degrees C and then incubating it at the same temperature. Thus, metarhodopsin II or an earlier intermediate than metarhodopsin II should be a direct intermediate for the enzyme activation.

MeSH Terms
3',5'-Cyclic-GMP Phosphodiesterases/metabolism Animals Cell Membrane/enzymology Chickens Enzyme Activation Kinetics Photoreceptor Cells/enzymology Protein Binding Rana catesbeiana Retinal Pigments/pharmacology Rhodopsin/analogs & derivatives,pharmacology Rod Cell Outer Segment/enzymology
Chemicals
Retinal Pigments Rhodopsin 3',5'-Cyclic-GMP Phosphodiesterases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Yoshizawa T
Fukada Y
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28 references, click to expand
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Article Info
Journal
Biophysics of structure and mechanism
Abbr.
Biophys Struct Mech
ISSN
0340-1057
Published
1983-00-00
Pages
245-58
Language
English
Region
Germany
NLM ID
7502020
Subset
IM
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