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Heme as an allosteric regulator in C...

Parks, Ryan Brett.

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Heme as an allosteric regulator in CooA and cystathionine beta-synthase.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Heme as an allosteric regulator in CooA and cystathionine beta-synthase./
Author:	Parks, Ryan Brett.
Description:	189 p.
Notes:	Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1819.
Contained By:	Dissertation Abstracts International63-04B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3049353
ISBN:	0493638997

Heme as an allosteric regulator in CooA and cystathionine beta-synthase.
Parks, Ryan Brett.

Heme as an allosteric regulator in CooA and cystathionine beta-synthase. - 189 p.

Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1819.

Thesis (Ph.D.)--The University of Wisconsin - Madison, 2002.

CooA is a bacterial transcription factor employing a heme moiety to sense carbon monoxide. Found in <italic>Rhodospirillum rubrum</italic>, CooA is the only protein known to sense CO. Characterization of the heme was accomplished using electron paramagnetic resonance, electronic absorption, resonance Raman, and fluorescence spectroscopies in conjunction with ligand binding studies. In addition to CO, CooA binds NO, resulting in a five-coordinate nitrosyl heme, which does not activate the protein as CO does. Furthermore, metalloporphyrin substituted analogs of CooA are proposed, to provide a better definition of the heme coordination environment by determining the coordination requirements for allosteric change. An exploration into possible hydrogen bonding near the heme was initiated in order to define likely protein interactions involved in the allostery of CooA. As the site for CO-sensing, the heme holds the key to understanding the origin of the allosteric conformational changes of CooA.

ISBN: 0493638997Subjects--Topical Terms:

586156
Chemistry, Analytical.

Heme as an allosteric regulator in CooA and cystathionine beta-synthase.
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100 1 $a Parks, Ryan Brett. $3 1259082
245 1 0 $a Heme as an allosteric regulator in CooA and cystathionine beta-synthase.
300 $a 189 p.
500 $a Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1819.
500 $a Supervisor: Judith N. Burstyn.
502 $a Thesis (Ph.D.)--The University of Wisconsin - Madison, 2002.
520 $a CooA is a bacterial transcription factor employing a heme moiety to sense carbon monoxide. Found in <italic>Rhodospirillum rubrum</italic>, CooA is the only protein known to sense CO. Characterization of the heme was accomplished using electron paramagnetic resonance, electronic absorption, resonance Raman, and fluorescence spectroscopies in conjunction with ligand binding studies. In addition to CO, CooA binds NO, resulting in a five-coordinate nitrosyl heme, which does not activate the protein as CO does. Furthermore, metalloporphyrin substituted analogs of CooA are proposed, to provide a better definition of the heme coordination environment by determining the coordination requirements for allosteric change. An exploration into possible hydrogen bonding near the heme was initiated in order to define likely protein interactions involved in the allostery of CooA. As the site for CO-sensing, the heme holds the key to understanding the origin of the allosteric conformational changes of CooA.
520 $a Cystathionine β-synthase (CBS) is a heme-containing enzyme that plays a role in the transsulfuration pathway. CBS catalyzes the breakdown of toxic homocysteine, which can cause severe pathologies in humans (e.g. dislocation of the optic lens, thrombosis, osteoporosis, and mental retardation) and has been implicated in the progression of Alzheimer's disease. Mammalian CBS contains a heme group of unknown function that has a His/Cys ligation. A truncated catalytic core fragment of the enzyme, called CBS-45, has been overexpressed and provided to us by Dr. Jan Kraus. A full spectroscopic characterization of the heme in CBS-45 is presented using data from electron paramagnetic resonance, electronic absorption, and magnetic circular dichroism spectroscopies in combination with ligand binding studies. The reduced form shows pH dependence at the heme, shifting from six- to five-coordinate via the loss of the cysteine ligand. Only the five-coordinate heme is capable of binding both CO and NO. The heme may serve an allosteric function in CBS, where the active form of the enzyme requires the heme to be six-coordinate with cysteine bound.
590 $a School code: 0262.
650 4 $a Chemistry, Analytical. $3 586156
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Chemistry, Inorganic. $3 517253
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690 $a 0488
710 2 0 $a The University of Wisconsin - Madison. $3 626640
773 0 $t Dissertation Abstracts International $g 63-04B.
790 $a 0262
790 1 0 $a Burstyn, Judith N., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3049353