APO-SUPEROXIDE DISMUTASE SOLUTION STRUCTURE

APO-超氧化物歧化酶溶液结构

• 批准号: 8168975
• 负责人: JAMES W WHITTAKER
• 金额: $ 0.94万
• 依托单位: UNIVERSITY OF WISCONSIN-MADISON
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-03-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8168975
• 关键词: Antioxidants; Binding; Biological; Biological Process; Chemistry; Computer Retrieval of Information on Scientific Projects Database; Disease; Enzymes; Funding; Goals; Grant; Health; Human; Institution; Ions; Light; Manganese; Manganese Catalase; Manganese Superoxide Dismutase; Metals; Molecular; Neurodegenerative Disorders; Oxidation-Reduction; Oxidative Stress; Research; Research Personnel; Resources; Role; Solutions; Source; Structure; Superoxide Dismutase; United States National Institutes of Health; Work; insight; metalloenzyme; oxalate oxidase; trafficking

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. Manganese redox chemistry is fundamental to biological processes at molecular,cellular and environmental scales, from antioxidant defense to oxygenicphotosynthesis. Biomedically important enzymes including Mn superoxide dismutase(MnSOD), Mn catalase (MnC), and oxalate oxidase (OXO) require a catalytic manganesecofactor for their biological function, yet the molecular mechanisms involved indelivering the essential metal ion are just beginning to be studied in detail. The goal of this project is to advance our understanding of the biochemicalmechanisms responsible for the metal-binding maturation of the ubiquitous andessential antioxidant metalloezyme, MnSOD. This work is fundamental to understandingthe role of manganese trafficking in human health and disease. Further,understanding the metal binding mechanism of this Mn metalloenzyme may contributenew insight into biological defenses against oxidative stress, a key factor in agingand neurodegenerative disorders. This work may also shed light on diseases of metalhomeostasis in which metal misincorporation occurs.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 中心，不一定是研究者的机构。 锰氧化还原化学对于分子、细胞和环境尺度的生物过程（从抗氧化防御到产氧光合作用）至关重要。 生物医学上重要的酶，包括锰超氧化物歧化酶 (MnSOD)、锰过氧化氢酶 (MnC) 和草酸氧化酶 (OXO)，其生物学功能需要催化锰辅助因子，但传递必需金属离子的分子机制才刚刚开始详细研究。 该项目的目标是加深我们对普遍存在且必需的抗氧化剂金属酶 MnSOD 金属结合成熟的生化机制的理解。这项工作对于了解锰贩运在人类健康和疾病中的作用至关重要。 此外，了解这种锰金属酶的金属结合机制可能有助于对氧化应激的生物防御提供新的见解，氧化应激是衰老和神经退行性疾病的关键因素。这项工作还可能揭示发生金属错误掺入的金属稳态疾病。