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O2 ACTIVATION BY MOSSBAUER SPECTROSCOPY

通过穆斯鲍尔光谱法激活 O2

基本信息

批准号：
6518926
负责人：
ECKARD MUNCK
金额：
$ 26.83万
依托单位：
CARNEGIE-MELLON UNIVERSITY
依托单位国家：
美国
项目类别：
财政年份：
1990
资助国家：
美国
起止时间：
1990-05-01 至 2003-04-30
项目状态：
已结题

项目摘要

This proposal seeks to elucidate the structure and function of a variety of iron-containing enzymes involved in oxygen activation and acetate synthesis. Moreover, it is proposed to investigate the electronic structure of synthetic complexes that mimic structural and electronic features of the enzymes under study. The experimental techniques employed are 57Fe Mossbauer spectroscopy, Electron Paramagnetic Resonance and SQUID magnetometry. (1) Studies of the diiron proteins methane monooxygenase, ribonucleotide reductase, delta9 desaturase, toluene monooxygenase, phenol hydroxylase and alkane hydroxylase will be continued with particular focus on characterizing the electronic structure of catalytic intermediates. (2) This research will be complemented by studies of model complexes to gain insight into the electronic structure of the active sites of the enzymes. (3) Studies of FNR transcription factor as isolated and in whole E.coli cells will be continued. (4) Mossbauer studies of 1-aminopropane-1-carboxylate oxidase from avocado, cloned into E. coli, will be performed. (5) The Collins laboratory at Carnegie Mellon University has designed a variety of iron-containing complexes that are potent catalysts for dye and pulp bleaching, and that have high promise in green chemistry. The high- valent states of these complexes will be investigated with the goal of characterizing their catalytic behavior. These complexes are also of interest as spectroscopic benchmarks for FeIV states in proteins. (6) Experimental and theoretical studies of the structure the Nickel- [4Fe-4S] cluster assemblies of carbon monoxide dehydrogenases isolated from Clostridium thermoaceticum and Rhodospirillum rubrum will be continued. These studies will be extended to iron-hydrogenases which appear to have a cluster assembly involving a[4Fe4S] cluster as well.

该建议旨在阐明参与氧活化和乙酸合成的各种含铁酶的结构和功能。此外，它建议调查的电子结构的合成复合物，模仿所研究的酶的结构和电子特征。所采用的实验技术是57 Fe穆斯堡尔谱，电子顺磁共振和SQUID磁强计。 (1)二铁蛋白质甲烷单加氧酶，核糖核苷酸还原酶，delta 9去饱和酶，甲苯单加氧酶，苯酚羟化酶和烷烃羟化酶的研究将继续特别侧重于表征催化中间体的电子结构。 (2)这项研究将通过模型复合物的研究来补充，以深入了解酶活性位点的电子结构。 (3)FNR转录因子的分离和在整个大肠杆菌细胞中的研究将继续进行。 (4)用穆斯堡尔谱研究了鳄梨1-氨基丙烷-1-羧酸氧化酶的结构。大肠杆菌，将进行。 (5)卡内基梅隆大学的柯林斯实验室设计了各种含铁络合物，它们是染料和纸浆漂白的有效催化剂，在绿色化学中具有很高的前景。这些配合物的高价态将被研究，目的是表征它们的催化行为。这些复合物也感兴趣的光谱基准FeIV状态的蛋白质。 (6)从Clostridium thermoaceticum和Rhodocellum rubrum分离的一氧化碳脱氢酶的镍- [4Fe-4S]簇组装体的结构的实验和理论研究将继续进行。这些研究将扩展到铁氢化酶似乎有一个集群组装涉及一个[4Fe 4S]集群以及。

项目成果

期刊论文数量（41）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 2. Mössbauer spectroscopy.

亚硝化单胞菌羟胺氧化还原酶的多个血红素中心的分离。

DOI：
10.1021/bi00260a011
发表时间：
1982
期刊：
Biochemistry
影响因子：
2.9
作者：
Lipscomb,JD;Andersson,KK;Münck,E;Kent,TA;Hooper,AB
通讯作者：
Hooper,AB

Properties of a copper-containing cytochrome ba3: a second terminal oxidase from the extreme thermophile Thermus thermophilus.

DOI：
10.1073/pnas.85.16.5779
发表时间：
1988-08
期刊：
Proceedings of the National Academy of Sciences of the United States of America
影响因子：
11.1
作者：
B. Zimmermann;C. Nitsche;J. Fee;F. Rusnak;E. Münck
通讯作者：
B. Zimmermann;C. Nitsche;J. Fee;F. Rusnak;E. Münck

Brevibacterium fuscum protocatechuate 3,4-dioxygenase. Purification, crystallization, and characterization.

DOI：
10.1016/s0021-9258(17)43071-7
发表时间：
1984-04
期刊：
The Journal of biological chemistry
影响因子：
0
作者：
J. W. Whittaker;J. Lipscomb;T. Kent;E. Münck
通讯作者：
J. W. Whittaker;J. Lipscomb;T. Kent;E. Münck

Mössbauer and electron nuclear double resonance study of oxidized bidirectional hydrogenase from Clostridium pasteurianum W5.

巴氏梭菌 W5 氧化双向氢化酶的穆斯堡尔和电子核双共振研究。

DOI：
发表时间：
1984
期刊：
The Journal of biological chemistry
影响因子：
0
作者：
Wang,G;Benecky,MJ;Huynh,BH;Cline,JF;Adams,MW;Mortenson,LE;Hoffman,BM;Münck,E
通讯作者：
Münck,E

Interconversions of [3Fe-3S] and [4Fe-4S] clusters. Mössbauer and electron paramagnetic resonance studies of Desulfovibrio gigas ferredoxin II.

[3Fe-3S] 和 [4Fe-4S] 团簇的相互转化。