RIFTIA HEMOGLOBIN

RIFTIA血红蛋白

• 批准号: 7602314
• 负责人: WILLIAM E ROYER
• 金额: $ 0.31万
• 依托单位: BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-07-01 至 2008-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7602314
• 关键词: Bacteria; Binding; Biochemical; Computer Retrieval of Information on Scientific Projects Database; Condition; Cysteine; Data Collection; Depth; Funding; Grant; Hemoglobin; Institution; Ions; Life; Localized; Oxygen; Property; Research; Research Personnel; Resolution; Resources; Sea; Source; Structure; Sulfides; Synchrotrons; Testing; United States National Institutes of Health; Zinc; novel; research study

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. The 400kDa hemoglobin from the deep-sea tubeworm, Riftia pachyptila, has the remarkable property of transporting both oxygen and sulfide to the chemoautotrophic bacteria that live in its gut. Our crystal structure of this molecule (Flores et al., 2005, Proc. Natl. Acad. Sci. 102, 2713-2718) revealed both a novel assembly of subunits and unexpected bound zinc ions. We have carried out biochemical experiments that suggest, contrary to the prevailing dogma, that these zinc ions are directly involved in binding sulfide. In order to test this hypothesis, and the alternative one suggesting binding at cysteine residues, we have grown crystals of this molecule in the presence of sulfide under anaerobic conditions. Synchrotron diffraction data collection is required to obtain sufficient resolution from these crystals to permit localizing bound sulfide.

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。子项目和 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 对于中心来说，它不一定是研究者的机构。 来自深海管虫 Riftia pachyptila 的 400kDa 血红蛋白具有将氧气和硫化物运输到其肠道内的化学自养细菌的显着特性。 我们对该分子的晶体结构（Flores et al., 2005, Proc. Natl. Acad. Sci. 102, 2713-2718）揭示了一种新颖的亚基组装和意想不到的结合锌离子。 我们进行的生化实验表明，与普遍的教条相反，这些锌离子直接参与结合硫化物。 为了测试这一假设以及表明在半胱氨酸残基上结合的另一种假设，我们在硫化物存在的情况下在厌氧条件下生长了该分子的晶体。 需要同步加速器衍射数据收集来从这些晶体获得足够的分辨率，以允许定位结合的硫化物。