Cation effects on the purple membrane of Halobacterium halobium
type: CreativeWork
description: 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.
abstract: 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.
author: Jonas, Roy Edward
language: eng
keywords: Biophysics, General
date published: 2011-05-07T12:32:14Z
date modified: 2026-07-22T22:25:15Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/20207