XAS COPPER CONTAINING MONOOXYGENASE ENZYMES & RELEVANT INORGANIC MODEL COMPOUNDS

XAS 含铜单加氧酶

• 批准号: 6586701
• 负责人: Ninian J Blackburn
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586701
• 关键词: biological products; biomaterials; biomedical resource; proteins; spectrometry; structural biology

Two important monooxygenase enzymes, dopamine-b-hydroxylase (DBH) and peptidylglycine hydroxylating monooxygenase (PHM) are involved in the biosynthesis of neurotransmitters and peptide hormones, and are thus of pivotal importance in cell signalling mechanisms, and neuroregulatory function. The research is focussed toward elucidating the coordination chemistry of the Cu(I) forms of the enzymes, at which dioxygen-binding and substrate hydroxylation occur. Novel methodologies involving binding of Cu(I)-specific ligands such as CO and isocyanides will be developed as powerful probes of Cu(I) structure and substitution chemistry. Site directed mutants of PHM will also be studied in order to test current models of active-site structure.

两种重要的单加氧酶，多巴胺-b-羟化酶 (DBH) 和肽基甘氨酸羟化单加氧酶 (PHM) 参与 神经递质和肽激素的生物合成， 因此在细胞信号传导机制中至关重要，并且 神经调节功能。 该研究的重点是阐明 酶的 Cu(I) 形式的配位化学，其中 发生双氧结合和底物羟基化。 小说 涉及结合 Cu(I) 特异性配体（例如 CO）的方法 异氰化物将被开发为 Cu(I) 的强大探针 结构和取代化学。 PHM 的定点突变体 还将进行研究，以测试当前的活动站点模型 结构。