RIFTIA HEMOGLOBIN

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 来自深海管虫Riftia pachyptila的400 kDa血红蛋白具有将氧气和硫化物输送到生活在其肠道中的化学自养细菌的显著特性。我们对该分子的晶体结构(Flores等人，2005，Proc.娜塔莉。阿卡德。SCI。102,2713-2718)揭示了一种新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，与流行的教条相反，这些锌离子直接参与了硫化物的结合。为了验证这一假设，以及另一种认为半胱氨酸残基结合的假设，我们在厌氧条件下，在硫化物存在的情况下生长了这种分子的晶体。需要收集同步加速器衍射数据，以从这些晶体中获得足够的分辨率，以便定位结合硫化物。

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.