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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：
Amanda Byer
金额：
$ 6.98万
依托单位：
CORNELL UNIVERSITY
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：
https://reporter.nih.gov/project-details/10382228
关键词：
ATP phosphohydrolase Active Sites Address Affect Allosteric Regulation Anabolism Binding Sites Biochemical Biochemical Pathway Biochemistry Bioinformatics Biological Models Biological Process Biophysics Catalysis Chemistry Chlorophyll Complex Coupled Coupling Cryoelectron Microscopy Drug Targeting Electron Microscopy Electron Transport Electrons Enzymes Goals Hydrogenase Ions Iron Knowledge Length Life Metals Methods Mission Molecular Molecular Conformation Montana Motion Movement National Institute of General Medical Sciences Nature Nitrogenase Organism Outcome Oxidation-Reduction Oxidoreductase Oxygen Pharmaceutical Preparations Pharmacology Physiology Postdoctoral Fellow Property Protein Conformation Protein Subunits Proteins Reaction Regulation Research Roentgen Rays Role S-Adenosylmethionine Sampling Shapes Side Site Source Structure Sulfur Techniques Testing Tetrapyrroles Therapeutic Training Transition Elements United States National Institutes of Health Universities Variant active control chemical reaction design dimer evidence base improved interfacial metalloenzyme oxidation pi bond prevent response single bond structural biology technique development tool

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.

项目摘要/摘要