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J. Biol. Chem., Vol. 278, Issue 6, 4339-4346, February 7, 2003

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Purification of a Cytochrome bc₁-aa₃ Supercomplex with Quinol Oxidase Activity from Corynebacterium glutamicum
IDENTIFICATION OF A FOURTH SUBUNIT OF CYTOCHROME aa₃ OXIDASE AND MUTATIONAL ANALYSIS OF DIHEME CYTOCHROME c₁^*

Axel Niebisch and Michael Bott

From the Institut für Biotechnologie 1, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany

The aerobic respiratory chain of the Gram-positive Corynebacterium glutamicum involves a bc₁ complex with a diheme cytochrome c₁ and a cytochrome aa₃ oxidase but no additional c-type cytochromes. Here we show that the two enzymes form a supercomplex, because affinity chromatography of either strep-tagged cytochrome b (QcrB) or strep-tagged subunit I (CtaD) of cytochrome aa₃ always resulted in the copurification of the subunits of the bc₁ complex (QcrA, QcrB, QcrC) and the aa₃ complex (CtaD, CtaC, CtaE). The isolated bc₁-aa₃ supercomplexes had quinol oxidase activity, indicating functional electron transfer between cytochrome c₁ and the Cu_A center of cytochrome aa₃. Besides the known bc₁ and aa₃ subunits, few additional proteins were copurified, one of which (CtaF) was identified as a fourth subunit of cytochrome aa₃. If either of the two CXXCH motifs for covalent heme attachment in cytochrome c₁ was changed to SXXSH, the resulting mutants showed severe growth defects, had no detectable c-type cytochrome, and their cytochrome b level was strongly reduced. This indicates that the attachment of both heme groups to apo-cytochrome c₁ is not only required for the activity but also for the assembly and/or stability of the bc₁ complex.

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