Examining the Proton Channels in Heme -Copper Oxidases
Tomson, Farol Lovell
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https://hdl.handle.net/2142/84781
Description
Title
Examining the Proton Channels in Heme -Copper Oxidases
Author(s)
Tomson, Farol Lovell
Issue Date
2002
Doctoral Committee Chair(s)
Gennis, Robert B.
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
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.
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