Cytochrome aa 3 serves as a terminal oxidase in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. A procedure for its isolation is described. The purified preparation consists of only one major polypeptide of 38 kDa apparent molecular mass. The enzyme contains two heme α molecules with midpoint potentials of + 220 and + 370 mV, respectively. The copper content is at least 2 Cu/aa 3. It has only negligible capacity to oxidize cytochrome c, but rather serves as an oxidase for reduced caldariella quinone as present in the membrane of Sulfolobus.
No takes yet. Share an insight, caveat, or question.
Anemüller et al. (1989) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: