ATP5C1 Human

ATP synthase is a crucial enzyme found in the mitochondria, responsible for the synthesis of adenosine triphosphate (ATP), the primary energy carrier in cells. The enzyme operates by utilizing an electrochemical gradient of protons across the inner mitochondrial membrane during oxidative phosphorylation .

ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel . The catalytic portion of mitochondrial ATP synthase consists of five different subunits: alpha, beta, gamma, delta, and epsilon. These subunits are assembled with a stoichiometry of three alpha, three beta, and a single representative of the other three .

The gamma subunit, encoded by the ATP5C1 gene, plays a pivotal role in the catalytic core of ATP synthase. It is involved in the rotational mechanism that drives ATP synthesis . The gamma subunit interacts with the alpha and beta subunits, facilitating the conformational changes necessary for ATP production .

The human recombinant ATP synthase gamma chain is typically produced in Escherichia coli (E. coli) expression systems. The recombinant protein is often fused to a His-tag at the N-terminus to facilitate purification through affinity chromatography . The purified protein is used in various research applications, including structural and functional studies of ATP synthase .

Recombinant ATP synthase gamma chain is used in research to understand the enzyme’s mechanism and its role in cellular energy metabolism. It is also employed in studies investigating mitochondrial diseases and potential therapeutic interventions .