SINGLE CRYSTAL XAS STUDIES OF HEME CATALYSIS
血红素催化的单晶 XAS 研究
基本信息
- 批准号:8169949
- 负责人:
- 金额:$ 0.34万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2010
- 资助国家:美国
- 起止时间:2010-05-01 至 2011-02-28
- 项目状态:已结题
- 来源:
- 关键词:BindingCamphorCatalysisChemicalsComputer Retrieval of Information on Scientific Projects DatabaseCrystallographyCytochrome P450Cytochrome c PeroxidaseElectronicsElectronsEnzymesFundingGrantHemeHydrogen PeroxideHydroxylationInstitutionLigandsMolecular ConformationNatureOxidation-ReductionOxygenPseudomonas putidaResearchResearch PersonnelResourcesRestSaccharomyces cerevisiaeSourceSpectrum AnalysisStructureSystemUnited States National Institutes of Healthmolecular vectoroxidationprogramsvector
项目摘要
This subproject is one of many research subprojects utilizing the
resources provided by a Center grant funded by NIH/NCRR. The subproject and
investigator (PI) may have received primary funding from another NIH source,
and thus could be represented in other CRISP entries. The institution listed is
for the Center, which is not necessarily the institution for the investigator.
We plan to utilize single crystal XAS to study two representative heme-containing enzymes?cytochrome P450 from Pseudomonas putida, which catalyzes the regio- and stereo-specific hydroxylation of camphor, and cytochrome c peroxidase from Saccharomyces cerevisiae, which catalyzes the two-electron oxidation of hydrogen peroxide. Like most Fe-heme enzymes, these are thought to go through several Fe-oxo intermediates, including an oxy-ferryl state (compound I), as part of their catalytic cycle. Although, these enzymes have been extensively characterized by both crystallography and spectroscopy, questions still remain about the nature of their reactive intermediates. By examining stable, metastable, and radiolytically reduced states of these enzymes using Fe K-edge single crystal XAS, we plan to characterize the structure of their catalytic intermediates through EXAFS analysis concomitant with electronic state determination through analysis of the edge region. Single crystal XAS can be used in anisotropic systems to selectively enhance specific molecular vectors through crystallographic alignment with the beam polarization vector, thereby providing enhanced geometric and electronic details about a molecule. In the cytochrome P450 study, polarized XAS will be used to probe the axial Fe-substrate oxygen and Fe-proximal ligand interactions separately from the Fe-heme interactions. The program outlined herein should provide for a detailed understanding of heme enzyme catalysis through 1) the polarized single crystal XAS study of wild-type and effector bound conformations of cytochrome P450 in the resting state and, potentially, in six other forms produced by camphor incubation, chemical oxidation/reduction, oxygenation, and radiolytic reduction; and 2) the single crystal XAS study of cytochrome c peroxidase in the ferric resting-state, ferryl compound I state, and in the radiolytically generated products of the compound I state.
这个子项目是许多研究子项目中的一个
由NIH/NCRR资助的中心赠款提供的资源。子项目和
研究者(PI)可能从另一个NIH来源获得了主要资金,
因此可以在其他CRISP条目中表示。所列机构为
研究中心,而研究中心不一定是研究者所在的机构。
我们计划利用单晶XAS研究两个代表性的血红素含酶?来自恶臭假单胞菌的细胞色素P450,其催化樟脑的区域和立体特异性羟基化,和来自酿酒酵母的细胞色素c过氧化物酶,其催化过氧化氢的双电子氧化。与大多数铁血红素酶一样,这些酶被认为通过几种铁氧中间体,包括氧铁基状态(化合物I),作为其催化循环的一部分。虽然,这些酶已被广泛的晶体学和光谱学的特点,问题仍然存在关于其活性中间体的性质。通过检查稳定的,亚稳态的,这些酶的放射性还原状态,使用铁K-边缘单晶XAS,我们计划通过EXAFS分析伴随着电子状态的测定,通过分析的边缘区域来表征其催化中间体的结构。单晶XAS可用于各向异性系统中,以通过与光束偏振矢量的晶体学对准来选择性地增强特定的分子矢量,从而提供关于分子的增强的几何和电子细节。在细胞色素P450研究中,极化XAS将用于分别探测轴向Fe-底物氧和Fe-近端配体相互作用与Fe-血红素相互作用。本文概述的程序应该通过1)细胞色素P450在静止状态下和潜在地在由樟脑孵育、化学氧化/还原、氧合和辐射分解还原产生的六种其它形式下的野生型和效应物结合构象的极化单晶XAS研究提供对血红素酶催化的详细理解;和2)在铁静止态、铁基化合物I态和化合物I态的辐射分解产物中的细胞色素c过氧化物酶的单晶XAS研究。
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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BRITT HEDMAN其他文献
BRITT HEDMAN的其他文献
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{{ truncateString('BRITT HEDMAN', 18)}}的其他基金
A Synchrotron Radiation Structural Biology Resource
同步辐射结构生物学资源
- 批准号:
10350698 - 财政年份:2020
- 资助金额:
$ 0.34万 - 项目类别:
A Synchrotron Radiation Structural Biology Resource
同步辐射结构生物学资源
- 批准号:
10578809 - 财政年份:2020
- 资助金额:
$ 0.34万 - 项目类别:
SINGLE CRYSTAL XAS STUDIES ON O2 ACTIVATING HEME PROTEINS
O2 激活血红素蛋白的单晶 XAS 研究
- 批准号:
8362248 - 财政年份:2011
- 资助金额:
$ 0.34万 - 项目类别:
S K-EDGE XAS STUDIES AS A PROBE OF ELECTRONIC STRUCTURE/CONTRIBUTION TO FUNCTION
SK-EDGE XAS 研究作为电子结构/功能贡献的探针
- 批准号:
8362398 - 财政年份:2011
- 资助金额:
$ 0.34万 - 项目类别:
XAS COMPARISON OF NITROGENASE MOFE PROTEIN MUTANTS
固氮酶 MOFE 蛋白突变体的 XAS 比较
- 批准号:
8362047 - 财政年份:2011
- 资助金额:
$ 0.34万 - 项目类别:
INVESTIGATION OF ELECTRONIC STRUCTURES OF FE-S AND MO-S ACTIVE SITES AND THEIR R
FE-S和Mo-S活性位点的电子结构及其R的研究
- 批准号:
8362082 - 财政年份:2011
- 资助金额:
$ 0.34万 - 项目类别:
100-ELEMENT GE DETECTOR SYSTEM FOR X-RAY ABSORPTION SPECTROSCOPY
用于 X 射线吸收光谱的 100 元件 GE 探测器系统
- 批准号:
8362139 - 财政年份:2011
- 资助金额:
$ 0.34万 - 项目类别:
100-ELEMENT GE DETECTOR SYSTEM FOR X-RAY ABSORPTION SPECTROSCOPY
用于 X 射线吸收光谱的 100 元件 GE 探测器系统
- 批准号:
8170071 - 财政年份:2010
- 资助金额:
$ 0.34万 - 项目类别:
INVESTIGATION OF ELECTRONIC STRUCTURES OF FE-S AND MO-S ACTIVE SITES AND THEIR R
FE-S和Mo-S活性位点的电子结构及其R的研究
- 批准号:
8169978 - 财政年份:2010
- 资助金额:
$ 0.34万 - 项目类别:
SINGLE CRYSTAL XAS STUDIES OF NITROGENASE PROTEINS
固氮酶蛋白的单晶 XAS 研究
- 批准号:
8169950 - 财政年份:2010
- 资助金额:
$ 0.34万 - 项目类别:
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