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Wild-type and several mutants of cytochrome c oxidase from Rhodobacter sphaeroides were characterized by EPR spectroscopy. A pH-induced g12 signal, seen previously in mammalian cytochrome oxidase and assigned to the presence of a bridging car☐yl ligand in the bimetallic cytochrome a 3 -Cu B site, is found also in the bacterial enzyme. Mutation of glutamate-286 to glutamine inactivates...
A rapid and highly efficient method of purifying the aa 3 -type cytochrome c oxidase from Rhodobacter sphaeroides has been developed. This method relies upon a six-histidine affinity tag fused to the C-terminus of subunit I, which confers to the oxidase a high affinity for Ni 2+ -nitrilotriacetic acid (NTA) agarose. The histidine-tagged oxidase can be purified rapidly and with...
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