STRUCTURE OF THE HYDROGENASE FROM THIOCAPSA ROSEOPERSICINA

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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.