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Development of a mitochondrial membr...

Pelster, Lindsey Nicole.

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Development of a mitochondrial membrane biomimic for characterization of the electron transport chain metabolon bioelectrocatalysis.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Development of a mitochondrial membrane biomimic for characterization of the electron transport chain metabolon bioelectrocatalysis./
Author:	Pelster, Lindsey Nicole.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2016,
Description:	151 p.
Notes:	Source: Dissertation Abstracts International, Volume: 78-07(E), Section: B.
Contained By:	Dissertation Abstracts International78-07B(E).
Subject:	Analytical chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10193831
ISBN:	9781369566482

Development of a mitochondrial membrane biomimic for characterization of the electron transport chain metabolon bioelectrocatalysis.
Pelster, Lindsey Nicole.

Development of a mitochondrial membrane biomimic for characterization of the electron transport chain metabolon bioelectrocatalysis. - Ann Arbor : ProQuest Dissertations & Theses, 2016 - 151 p.

Source: Dissertation Abstracts International, Volume: 78-07(E), Section: B.

Thesis (Ph.D.)--The University of Utah, 2016.

The electron transport chain (ETC) is a major bioenergetic pathway that converts chemical energy into an electrochemical gradient to produce adenosine triphosphate (ATP). The enzymes form a supercomplex or metabolon of three enzymes that have implications of the electron flux and catalytic activity of the chain. The enzymes transfer electrons to convert energy which make it an important enzyme chain to study multi-enzyme cascades and complete oxidation of substrates in the bioelectrochemistry field. While many have studied the protein-protein, structural, and genetic implications of the enzymes, the bioelectrocatalysis of the ETC supercomplex needs to be explored. This research focuses on enzymatic immobilization with different materials, which is an important aspect that affects how bioelectrocatalysis can be studied on electrodes.

ISBN: 9781369566482Subjects--Topical Terms:

3168300
Analytical chemistry.

Development of a mitochondrial membrane biomimic for characterization of the electron transport chain metabolon bioelectrocatalysis.
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245 1 0 $a Development of a mitochondrial membrane biomimic for characterization of the electron transport chain metabolon bioelectrocatalysis.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2016
300 $a 151 p.
500 $a Source: Dissertation Abstracts International, Volume: 78-07(E), Section: B.
500 $a Adviser: Shelley D. Minteer.
502 $a Thesis (Ph.D.)--The University of Utah, 2016.
520 $a The electron transport chain (ETC) is a major bioenergetic pathway that converts chemical energy into an electrochemical gradient to produce adenosine triphosphate (ATP). The enzymes form a supercomplex or metabolon of three enzymes that have implications of the electron flux and catalytic activity of the chain. The enzymes transfer electrons to convert energy which make it an important enzyme chain to study multi-enzyme cascades and complete oxidation of substrates in the bioelectrochemistry field. While many have studied the protein-protein, structural, and genetic implications of the enzymes, the bioelectrocatalysis of the ETC supercomplex needs to be explored. This research focuses on enzymatic immobilization with different materials, which is an important aspect that affects how bioelectrocatalysis can be studied on electrodes.
520 $a In this dissertation work, different methods of immobilization of membrane enzymes were explored with carbon nanotubes and tethered lipid membranes to provide a hydrophobic environment for the direct bioelectrocatalysis. The carbon nanotubes and polymer combinations were studied to examine the relationship of the electrocatalysis of cofactors and the impact of the polymer on enzymatic activity. The last part of this dissertation work focused on the development of a mitochondrial inner membrane biomimic for the immobilization of the electron transport chain supercomplex. The bioelectrocatalysis of the supercomplex was studied in a tethered lipid bilayer that allowed for the activity with its substrate cytochrome c. This work provided a starting point to looking at the bioelectrocatalysis of the ETC supercomplex and fundamental implications of enzymatic cascades in bioelectrocatalysis.
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773 0 $t Dissertation Abstracts International $g 78-07B(E).
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