語系:
繁體中文
English
說明(常見問題)
回圖書館首頁
手機版館藏查詢
登入
回首頁
到查詢結果
[ subject:"Chemistry, Biochemistry." ]
切換:
標籤
|
MARC模式
|
ISBD
Bacterial generation of the anti-gre...
~
The Ohio State University.
FindBook
Google Book
Amazon
博客來
Bacterial generation of the anti-greenhouse gas dimethylsulfide: Kinetic, spectroscopic, and computational studies of the DMSO reductase system.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Bacterial generation of the anti-greenhouse gas dimethylsulfide: Kinetic, spectroscopic, and computational studies of the DMSO reductase system./
作者:
Polsinelli, Gregory Anthony.
面頁冊數:
133 p.
附註:
Adviser: Ross Dalbey.
Contained By:
Dissertation Abstracts International68-12B.
標題:
Chemistry, Biochemistry. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3292738
ISBN:
9780549361473
Bacterial generation of the anti-greenhouse gas dimethylsulfide: Kinetic, spectroscopic, and computational studies of the DMSO reductase system.
Polsinelli, Gregory Anthony.
Bacterial generation of the anti-greenhouse gas dimethylsulfide: Kinetic, spectroscopic, and computational studies of the DMSO reductase system.
- 133 p.
Adviser: Ross Dalbey.
Thesis (Ph.D.)--The Ohio State University, 2008.
Biogenic dimethylsulfide (DMS) produced by marine microorganisms is the main source of sulfur thought to play a key role in cloud formation and global solar albedo. The study presented herein provides a better understanding of the global sulfur cycle at the molecular level by exploring the enzymatic process whereby DMS is generated from from dimethylsulfoxide (DMSO) by examining the pathway that leads to the generation of this gas, the DMSO reductase pathway.
ISBN: 9780549361473Subjects--Topical Terms:
1017722
Chemistry, Biochemistry.
Bacterial generation of the anti-greenhouse gas dimethylsulfide: Kinetic, spectroscopic, and computational studies of the DMSO reductase system.
LDR
:03247nam 2200301 a 45
001
856608
005
20100709
008
100709s2008 ||||||||||||||||| ||eng d
020
$a
9780549361473
035
$a
(UMI)AAI3292738
035
$a
AAI3292738
040
$a
UMI
$c
UMI
100
1
$a
Polsinelli, Gregory Anthony.
$3
1023435
245
1 0
$a
Bacterial generation of the anti-greenhouse gas dimethylsulfide: Kinetic, spectroscopic, and computational studies of the DMSO reductase system.
300
$a
133 p.
500
$a
Adviser: Ross Dalbey.
500
$a
Source: Dissertation Abstracts International, Volume: 68-12, Section: B, page: 8009.
502
$a
Thesis (Ph.D.)--The Ohio State University, 2008.
520
$a
Biogenic dimethylsulfide (DMS) produced by marine microorganisms is the main source of sulfur thought to play a key role in cloud formation and global solar albedo. The study presented herein provides a better understanding of the global sulfur cycle at the molecular level by exploring the enzymatic process whereby DMS is generated from from dimethylsulfoxide (DMSO) by examining the pathway that leads to the generation of this gas, the DMSO reductase pathway.
520
$a
Resonance Raman (rRaman) spectroscopic studies have also been undertaken in order to determine the roles of two active site residues, W116 and Y114, in the catalytic cycle of substrate turnover in DMSO reductase. We have found that whereas Y114F mutant forms a complex with DMSO substrate and W116F does not form the complex using multiple component analysis (MCA) and rRaman spectroscopy. The reaction mechanism of the properly redox cycled W116F form of the enzyme was determined and is reported.
520
$a
The physiological reductant of DMSO reductase is a pentaheme, membrane-bound c-type cytochrome protein known as DorC. The purification procedure for wild-type DorC has been successfully developed as part of this study. The limiting rate of electron transfer from DorC to DMSO reductase has been determined to be 2.66 s-1 using stopped-flow spectrophotometry and pseudo-first order reaction conditions. This experiment also yielded a Kd of 13.2 muM for binding of DorC to DMSOR. Electron paramagnetic resonance (EPR) spectroscopy has been used to analyze the possible generation of a Mo (V) intermediate and it does not appear as though a Mo (V) state is generated in the course of the reaction. Surface plasmon resonance (SPR or BIAcore) experiments have been undertaken to determine the dissociation constant (K d) of the complex independent of electron transfer. The Kd was determined to be approximately 30 muM.
520
$a
This study has also produced a computational model of DorC using the computer program Rosetta. From this model, protein docking simulations have been calculated using Hex 4.5 and have produced a compelling working model for the structure of the protein complex with a specific route of electron transfer from the five heme centers of DorC and into the molybdenum center of DMSO reductase identified.
590
$a
School code: 0168.
650
4
$a
Chemistry, Biochemistry.
$3
1017722
690
$a
0487
710
2
$a
The Ohio State University.
$3
718944
773
0
$t
Dissertation Abstracts International
$g
68-12B.
790
$a
0168
790
1 0
$a
Dalbey, Ross,
$e
advisor
791
$a
Ph.D.
792
$a
2008
856
4 0
$u
http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3292738
筆 0 讀者評論
館藏地:
全部
電子資源
出版年:
卷號:
館藏
1 筆 • 頁數 1 •
1
條碼號
典藏地名稱
館藏流通類別
資料類型
索書號
使用類型
借閱狀態
預約狀態
備註欄
附件
W9071817
電子資源
11.線上閱覽_V
電子書
EB W9071817
一般使用(Normal)
在架
0
1 筆 • 頁數 1 •
1
多媒體
評論
新增評論
分享你的心得
Export
取書館
處理中
...
變更密碼
登入