Structural Studies of Alternating-site Reactivity in Nitrogenase-like Oxidoreductases
固氮酶样氧化还原酶的交替位点反应性的结构研究
基本信息
- 批准号:10382228
- 负责人:
- 金额:$ 6.98万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2021
- 资助国家:美国
- 起止时间:2021-04-15 至 2024-04-14
- 项目状态:已结题
- 来源:
- 关键词:ATP phosphohydrolaseActive SitesAddressAffectAllosteric RegulationAnabolismBinding SitesBiochemicalBiochemical PathwayBiochemistryBioinformaticsBiological ModelsBiological ProcessBiophysicsCatalysisChemistryChlorophyllComplexCoupledCouplingCryoelectron MicroscopyDrug TargetingElectron MicroscopyElectron TransportElectronsEnzymesGoalsHydrogenaseIonsIronKnowledgeLengthLifeMetalsMethodsMissionMolecularMolecular ConformationMontanaMotionMovementNational Institute of General Medical SciencesNatureNitrogenaseOrganismOutcomeOxidation-ReductionOxidoreductaseOxygenPharmaceutical PreparationsPharmacologyPhysiologyPostdoctoral FellowPropertyProtein ConformationProtein SubunitsProteinsReactionRegulationResearchRoentgen RaysRoleS-AdenosylmethionineSamplingShapesSideSiteSourceStructureSulfurTechniquesTestingTetrapyrrolesTherapeuticTrainingTransition ElementsUnited States National Institutes of HealthUniversitiesVariantactive controlchemical reactiondesigndimerevidence baseimprovedinterfacialmetalloenzymeoxidationpi bondpreventresponsesingle bondstructural biologytechnique developmenttool
项目摘要
Project Summary / Abstract
Nature uses protein allostery to control long-range electron flow in chemical reactions essential
for life. Metals and metal-clusters are often key components facilitating this electron transfer. A
known allosteric method for gating electron flow in metalloenzymes is alternating-site reactivity,
wherein reactivity switches from one half of the enzyme to the other upon conformational
changes. Oxidoreductases, with a core α2β2 heterotetrameric structure, are iron-sulfur cluster
metalloenzymes that employ alternating-site reactivity and can serve as an invaluable model
system to define the structural motifs and mechanisms required for metalloenzyme allosteric
regulation. In line with the NIH NIGMS Pharmacology, Physiology, and Biochemical Chemistry
mission of “improving molecular level understanding of fundamental biological processes and
discovering approaches to their control”, we propose to study two such oxidoreductases, the
nitrogenase-like dark-operative chlorophyllide oxidoreductase (DPOR) and chlorophyllide
oxidoreductase (COR), to identify how long-ranged correlated motions contribute to alternating-
site reactivity using structural biology tools. We will employ electron microscopy and small-angle
X-ray scattering techniques to examine enzyme conformational intermediates with asymmetrical
conformations.
项目总结/摘要
大自然利用蛋白质变构来控制化学反应中的远程电子流动
终身金属和金属簇通常是促进这种电子转移的关键组分。一
已知用于在金属酶中门控电子流的变构方法是交替位点反应性,
其中当构象改变时,反应性从酶的一半切换到另一半,
变化氧化还原酶是一种以α2β2为核心的铁硫簇合物
金属酶,采用交替位点反应,可以作为一个宝贵的模型
定义金属酶变构所需的结构基序和机制的系统
调控根据NIH NIGMS药理学、生理学和生化学
使命是“提高对基本生物过程的分子水平理解,
发现控制它们的方法”,我们建议研究两种这样的氧化还原酶,
固氮酶样暗操作叶绿素氧化还原酶(DPOR)和叶绿素
氧化还原酶(COR),以确定长期相关的运动如何有助于交替-
使用结构生物学工具的位点反应性。我们将使用电子显微镜和小角度
X射线散射技术检测具有不对称构象的酶构象中间体
构象
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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Amanda Byer其他文献
Amanda Byer的其他文献
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{{ truncateString('Amanda Byer', 18)}}的其他基金
Structural Studies of Alternating-site Reactivity in Nitrogenase-like Oxidoreductases
固氮酶样氧化还原酶的交替位点反应性的结构研究
- 批准号:
10157289 - 财政年份:2021
- 资助金额:
$ 6.98万 - 项目类别:
Structural Studies of Alternating-site Reactivity in Nitrogenase-like Oxidoreductases
固氮酶样氧化还原酶的交替位点反应性的结构研究
- 批准号:
10592277 - 财政年份:2021
- 资助金额:
$ 6.98万 - 项目类别:
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