ACTIVE SITES OF FREE RADICAL METALLOENZYMES
自由基金属酶的活性位点
基本信息
- 批准号:2468897
- 负责人:
- 金额:$ 15.86万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:1992
- 资助国家:美国
- 起止时间:1992-02-01 至 2000-03-31
- 项目状态:已结题
- 来源:
- 关键词:Raman spectrometry X ray crystallography active sites atomic absorption spectrometry chemical kinetics chemical structure function circular dichroism copper electron spin resonance spectroscopy enzyme complex enzyme mechanism enzyme model free radicals galactose oxidase metal complex metalloenzyme protonation
项目摘要
DESCRIPTION: Free radical reactivity resulting from the ease of making
and breaking one electron bonds leads to essential roles for radicals
in biological catalysis, providing easy paths for fundamental processes
like C-C bond formation and cleavage, atom transfer and redox chemistry.
Biology has evolved specialized structures to take advantage of this
unique reactivity, but the instability of most biological radicals makes
them difficult to study in detail. The Whittaker's research is focused
on studies of an unusually stable free radical in the active site of
galactose oxidase, a protein radical directly participating in active
site redox chemistry as a free radical-coupled copper complex. Galactose
oxidase has provided a unique opportunity to study the involvement of
free radicals in enzyme catalysis, serving as a paradigm for radical
catalysis in other systems where the catalytic free radical is less
accessible. The research plan is based on a multidisciplinary approach
combining biochemistry, synthesis, spectroscopy, and computational
methods that give insight into the biological control of radical
reactivity. Mechanistic studies including isotope kinetics will explore
the role of protons in radical catalysis. Biochemical characterization
of galactose oxidase and two functional variants, glyoxol oxidase and
glycerol oxidase, will provide a framework for comparing the structure
and function of the radicals in these proteins. The comparative anatomy
of glyoxal oxidase will be developed through crystallographic and
mechanistic studies on wild type and mutant protein. Spectroscopic
studies (absorption, circular dichroism (CD), magnetic circular
dichroism (MCD), Stark, and electron paramagnetic resonance (EPR) will
extend structural information on the essential radicals to the
electronic level that relates directly to the origins of chemical
reactivity. Low temperature MCD experiments on the active site cupric
ion and inorganic models will extend insight into the role of the metal
in catalysis. These multiple experimental approaches will be
complemented by theoretical modeling of the spectra and ab initio
calculations of the electronic structure of the catalytic radical
complex.
说明:自由基的反应性使其易于制造
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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JAMES W WHITTAKER其他文献
JAMES W WHITTAKER的其他文献
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{{ truncateString('JAMES W WHITTAKER', 18)}}的其他基金
NMR SPECTROSCOPY OF APO-SUPEROXIDE DISMUTASE
载脂蛋白超氧化物歧化酶的核磁共振波谱
- 批准号:
8361261 - 财政年份:2011
- 资助金额:
$ 15.86万 - 项目类别:
TRAINING IN THE USE OF BRUKER AND VARIAN SPECTROMETERS AND NMR
布鲁克和瓦里安光谱仪和核磁共振的使用培训
- 批准号:
8361237 - 财政年份:2011
- 资助金额:
$ 15.86万 - 项目类别:
MOLECULAR BIOLOGY & ELECTRONIC STRUCTURES OF METALLO ENZYMES
分子生物学
- 批准号:
6221018 - 财政年份:1999
- 资助金额:
$ 15.86万 - 项目类别:
MOLECULAR BIOLOGY & ELECTRONIC STRUCTURES OF METALLOENZYMES
分子生物学
- 批准号:
6253499 - 财政年份:1997
- 资助金额:
$ 15.86万 - 项目类别:
Active Site Mechanisms of Free Radical Metalloenzymes
自由基金属酶的活性位点机制
- 批准号:
6430566 - 财政年份:1992
- 资助金额:
$ 15.86万 - 项目类别:
Active Site Mechanisms of Free Radical Metalloenzymes
自由基金属酶的活性位点机制
- 批准号:
6525643 - 财政年份:1992
- 资助金额:
$ 15.86万 - 项目类别:
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