Cation effects on the purple membrane of Halobacterium halobium

My more recent research shows that the binding of one divalent cation is directly related to the blue-to-purple transition of bacteriorhodopsin; whereas, four other divalent cation binding sites involving carboxyl groups on the bacteriorhodopsin surface do not directly affect the color change. The intrinsic pK$\sb{\rm a}$ of the binding of the special divalent cation and of the color transition is at about pH 2. The events involve the exchange of one divalent cation for two protons; I suggest that the two groups which release a proton upon binding of the divalent cation are aspartates-85 and -212 in the bacteriorhodopsin active site.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biophysics

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Jonas, Roy Edward

Contributors dc:contributor

• Ebrey, Thomas G.

• Biophysics, General

Statement dc:rights

• Copyright 1991 Jonas, Roy Edward

Language dc:language

eng

Identifier

AAI9210852
(UMI)AAI9210852

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/20207