Literature DB >> 6429947

Pathways in the hydrolysis of vertebrate rhodopsin.

C Blazynski, S E Ostroy.   

Abstract

A direct method for measuring the amount of retinal 387 was used along with spectral techniques to measure each of the intermediates in the photolysis of rhodopsin and to unequivocally determine the pathways in solution extracts of bovine rhodopsin and excised toad and skate retinas. Metarhodopsin II 380 was the earliest intermediate which hydrolyzed to retinal 387 plus opsin. In excised toad retinas three approaches were used to show that Meta III 465 decayed directly to retinal 387 plus opsin. The only pathway consistent with the data was: (Formula: See text). In solution extracts the formation and hydrolysis of N-Retinylidene-Opsin was also observed.

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Year:  1984        PMID: 6429947     DOI: 10.1016/0042-6989(84)90043-9

Source DB:  PubMed          Journal:  Vision Res        ISSN: 0042-6989            Impact factor:   1.886


  7 in total

1.  Function of the farnesyl moiety in visual signalling.

Authors:  N E McCarthy; M Akhtar
Journal:  Biochem J       Date:  2000-04-01       Impact factor: 3.857

2.  Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II.

Authors:  Martin Heck; Sandra A Schädel; Dieter Maretzki; Franz J Bartl; Eglof Ritter; Krzysztof Palczewski; Klaus Peter Hofmann
Journal:  J Biol Chem       Date:  2002-11-09       Impact factor: 5.157

3.  Structural comparison of metarhodopsin II, metarhodopsin III, and opsin based on kinetic analysis of Fourier transform infrared difference spectra.

Authors:  A L Klinger; M S Braiman
Journal:  Biophys J       Date:  1992-11       Impact factor: 4.033

4.  Rapid release of retinal from a cone visual pigment following photoactivation.

Authors:  Min-Hsuan Chen; Colleen Kuemmel; Robert R Birge; Barry E Knox
Journal:  Biochemistry       Date:  2012-05-07       Impact factor: 3.162

5.  Measurement of dipolar couplings in a transducin peptide fragment weakly bound to oriented photo-activated rhodopsin.

Authors:  B W Koenig; D C Mitchell; S König; S Grzesiek; B J Litman; A Bax
Journal:  J Biomol NMR       Date:  2000-02       Impact factor: 2.835

6.  Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.

Authors:  F F Davidson; P C Loewen; H G Khorana
Journal:  Proc Natl Acad Sci U S A       Date:  1994-04-26       Impact factor: 11.205

7.  Water permeation through the internal water pathway in activated GPCR rhodopsin.

Authors:  Katsufumi Tomobe; Eiji Yamamoto; Kholmirzo Kholmurodov; Kenji Yasuoka
Journal:  PLoS One       Date:  2017-05-11       Impact factor: 3.240

  7 in total

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