Complexity of Bovine Rhodopsin Activation Revealed at Low Temperature and Alkaline pH.

Abstract:

:The late intermediates involved in the activation mechanism of bovine rhodopsin are investigated by time-resolved optical absorption spectroscopy. Measurements from 10 μs to 200 ms after photolysis were carried out on membrane suspensions of bovine rhodopsin at a temperature of 15 °C and at pH of 7.3, 8.0, and 8.7. The time-resolved absorption spectra in the 330-650 nm range were analyzed by global exponential and kinetic scheme fitting methods. The results indicate an activation mechanism that is more complex than suggested previously. It involves interconnected branched pathways with two metarhodopsin I480 and two metarhodopsin II intermediates. The intermediates involved in this more complex mechanism need to be considered in spectroscopic studies that vary sample temperature and pH in order to enhance the presence of specific rhodopsin intermediates.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Szundi I,Funatogawa C,Kliger DS

doi

10.1021/acs.biochem.6b00687

subject

Has Abstract

pub_date

2016-09-13 00:00:00

pages

5095-105

issue

36

eissn

0006-2960

issn

1520-4995

journal_volume

55

pub_type

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