RIFTIA HEMOGLOBIN

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目及 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 来自深海管虫（Riftia pachyptila）的400 kDa血红蛋白具有将氧气和硫化物运输到生活在其肠道中的化能自养细菌的显着特性。 我们的这种分子的晶体结构（弗洛雷斯等人，2005，Proc. Natl. Acad. Sci. 102，2713-2718）揭示了亚基的新组装和意想不到的结合锌离子。 我们已经进行了生化实验，表明，与流行的教条相反，这些锌离子直接参与结合硫化物。 为了检验这一假设，以及另一个表明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下生长了该分子的晶体。 同步辐射衍射数据收集需要从这些晶体中获得足够的分辨率，以允许本地化绑定硫化物。

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.