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Electrochemical investigation of bac...

Ye, Tao.

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Electrochemical investigation of bacterial redox proteins.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Electrochemical investigation of bacterial redox proteins./
Author:	Ye, Tao.
Description:	233 p.
Notes:	Adviser: Sean J. Elliott.
Contained By:	Dissertation Abstracts International69-01B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3298692
ISBN:	9780549441427

Electrochemical investigation of bacterial redox proteins.
Ye, Tao.

Electrochemical investigation of bacterial redox proteins. - 233 p.

Adviser: Sean J. Elliott.

Thesis (Ph.D.)--Boston University, 2008.

This dissertation describes the electrochemical characterization of bacterial redox proteins, by the means of protein film voltammetry. Two distinct groups of proteins were examined, including electron-transfer proteins (the wild-type class I cytochromes c and corresponding mutants), and enzymes of multicopper oxidases (CueO and its mutants).

ISBN: 9780549441427Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Electrochemical investigation of bacterial redox proteins.
LDR:03349nam 2200313 a 45 001 942951
005 20110520
008 110520s2008 ||||||||||||||||| ||eng d
020 $a 9780549441427
035 $a (UMI)AAI3298692
035 $a AAI3298692
040 $a UMI $c UMI
100 1 $a Ye, Tao. $3 1259663
245 1 0 $a Electrochemical investigation of bacterial redox proteins.
300 $a 233 p.
500 $a Adviser: Sean J. Elliott.
500 $a Source: Dissertation Abstracts International, Volume: 69-01, Section: B, page: 0308.
502 $a Thesis (Ph.D.)--Boston University, 2008.
520 $a This dissertation describes the electrochemical characterization of bacterial redox proteins, by the means of protein film voltammetry. Two distinct groups of proteins were examined, including electron-transfer proteins (the wild-type class I cytochromes c and corresponding mutants), and enzymes of multicopper oxidases (CueO and its mutants).
520 $a Chapter 2 focuses on the role of Asn 64 (N64) of cytochrome c from Pseudomonas aeruginosa (PA) in determining the reduction potential, Em, by comparing it to the counterpart from Hydrogenobacter thermophilus (HT). It has been found that the hydrogen bonding of N64 to the distal methionine tunes the Em of the heme. As a result, replacing Asn with Gln lowers Em substantially in the N64Q mutant of the Pa protein, whereas, the Q64N of Ht has an increased E m. A homolog from Nitrosomonas europaea has been examined similarly and the result again implicates the importance of Met-donating loop residues in controlling Em.
520 $a Chapter 3 describes experiments that were also performed using a different set of variants, in which mutation was introduced at the proximal side. Data suggest that the redox properties of proteins are further influenced by the mobility of the heme-tethering loop. Changing the solvent accessibility to the heme pocket, evaluated through hydrogen exchange, has a strong impact upon the histidinate character of the axial ligand, which in turn determines the heme reduction potential. This correlation provides a framework to explain the pattern observed among mutants through NMR and electrochemical studies.
520 $a Chapter 4 concerns the impact of the electrode surface upon the adsorbed proteins. It has been observed that the edge plane of a pyrolytic graphite is able to preferentially populate protein species with open conformations, resulting in the new redox couple centered at -300mV the on the voltammogram.
520 $a CueO, described in Chapter 5, is a multi-copper oxidase that yields a catalytically competent protein film on a graphite or modified gold electrode surface. The pH profiles of catalytic wave resolved two redox transitions present at different pH regions and provided information regarding the intermediates species along the reaction pathway. Our current working hypothesis is that the intrinsic chemicakl/electrochemical step associated with the T1 center limits the overall turnover of Cue° Studies using M510L, a mutant with a modified T1 center support this idea.
590 $a School code: 0017.
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0487
710 2 $a Boston University. $3 1017454
773 0 $t Dissertation Abstracts International $g 69-01B.
790 $a 0017
790 1 0 $a Elliott, Sean J., $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3298692