Abstract 1472 Elucidating the role of Pet191 in the biogenesis of copper sites in cytochrome c oxidase

Mitochondrial cytochrome c oxidase (CcO) is a multisubunit heme-copper oxygen reductase equipped with several metal centers that are essential for its function. The enzyme harbors two copper binding centers– the heterobimetallic CuB center in the Cox1 subunit and the binuclear CuA center in the Cox2 subunit– that are assembled through a concerted action of dedicated metallochaperones and are the major sites of copper utilization in the organelle. Although CcO biogenesis is a relatively well-understood process, many details on the formation of the CuA and CuB centers are unclear.