APO-SUPEROXIDE DISMUTASE SOLUTION STRUCTURE

APO-超氧化物歧化酶溶液结构

• 批准号: 8361172
• 负责人: JAMES W WHITTAKER
• 金额: $ 0.25万
• 依托单位: UNIVERSITY OF WISCONSIN-MADISON
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361172
• 关键词: Antioxidants; Binding; Biological; Biological Process; Chemistry; Disease; Enzymes; Funding; Goals; Grant; Health; Human; Ions; Light; Manganese; Manganese Catalase; Manganese Superoxide Dismutase; Metals; Molecular; National Center for Research Resources; Neurodegenerative Disorders; Oxidation-Reduction; Oxidative Stress; Principal Investigator; Research; Research Infrastructure; Resources; Role; Solutions; Source; Structure; Superoxide Dismutase; United States National Institutes of Health; Work; cost; 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. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 从抗氧化防御到氧合光合作用，锰氧化还原化学在分子、细胞和环境尺度的生物过程中是基本的。生物医学上重要的酶，如锰超氧化物歧化酶(MnSOD)、锰过氧化氢酶(MNC)和草酸氧化酶(OXO)，其生物学功能需要一个催化的锰辅酶因子，但对其传递必需金属离子的分子机制的研究才刚刚开始。这个项目的目的是促进我们对金属结合成熟的生物化学机制的理解，这种金属酶是普遍存在的和必不可少的抗氧化剂金属酶，MnSOD。这项工作对于理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机制的新见解，氧化应激是衰老和神经退行性疾病的关键因素。这项工作也可能对发生金属错结合的代谢稳态疾病有所帮助。