Examining the Proton Channels in Heme -Copper Oxidases
type: CreativeWork
description: Previous work on the mutant enzyme KI-362M indicated that a block in the K-channel would result in the blockage of the catalytic cycle between the oxidized state and the two electron reduced state. This blockage occurs because an electron cannot enter the binuclear center without a proton to maintain the charge balance. If electrons cannot enter the binuclear center then the rate of reduction of the binuclear center is impaired. The E II-101 mutant enzymes had apparent first order rate constants, for the reduction of the binuclear center, between 0.56 and 15 s-1 compared to 159 s-1 for the wild-type enzyme. The measured rates of formation of other catalytic cycle intermediates were identical to wild-type. The data support the conclusion that EII-101 is the entrance to K-channel.
abstract: Previous work on the mutant enzyme KI-362M indicated that a block in the K-channel would result in the blockage of the catalytic cycle between the oxidized state and the two electron reduced state. This blockage occurs because an electron cannot enter the binuclear center without a proton to maintain the charge balance. If electrons cannot enter the binuclear center then the rate of reduction of the binuclear center is impaired. The E II-101 mutant enzymes had apparent first order rate constants, for the reduction of the binuclear center, between 0.56 and 15 s-1 compared to 159 s-1 for the wild-type enzyme. The measured rates of formation of other catalytic cycle intermediates were identical to wild-type. The data support the conclusion that EII-101 is the entrance to K-channel.
author: Tomson, Farol Lovell
language: eng
keywords: Chemistry, Biochemistry
date published: 2015-09-25T22:27:52Z
date modified: 2026-07-22T22:26:23Z
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/2142/84781