STRUCTURE OF THE HYDROGENASE FROM THIOCAPSA ROSEOPERSICINA

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的研究机构。 氢化酶是许多微生物体内H2代谢的关键酶，在全球生物氢循环中扮演着重要角色。 根据反应H2 = 2 H + +2 e-，它催化分子氢的可逆氧化还原。 [NiFe]氢化酶是一种膜结合多亚基复合物的组成部分，被认为是呼吸复合物I的祖先。 从嗜光细菌Thiocapsa roseopersicina（T.r.）是由一个大的64 kDa亚基和一个较小的34 kDa亚基组成的异二聚体。 T.R.氢化酶在该酶家族中是独特的，因为它与6个拷贝的异二聚体形成D3对称复合物。 我们的研究集中在氢化酶组装和催化的结构基础上。

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. Hydrogenase is the key enzyme in H2 metabolism in many microorganisms, and serves as an important player in global biological hydrogen cycling. It catalyzes reversible oxidoreduction of molecular hydrogen according to the reaction H2 = 2H+ + 2e-. The [NiFe] hydrogenase from Archaea and extremophiles functions as a component of a membrane-bound multisubunit complex, which has been thought of as the ancestor of the respiratory complex I. The [NiFe] hydrogenase from the phototropic bacterium Thiocapsa roseopersicina (T.r.) is a heterodimer composed of a large 64 kDa subunit and a smaller 34 kDa one. The T.r. hydrogenase is unique in this enzyme family in that it forms a D3 symmetric complex with 6 copies of the heterodimer. Our research is focused on the structural basis of hydrogenase assembly and catalysis.