Coordination of metal center biogenesis in human cytochrome c oxidase

Eva Nývltová, Jonathan V. Dietz, Javier Seravalli, Oleh Khalimonchuk and Antoni Barrientos ()
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Eva Nývltová: University of Miami Miller School of Medicine
Jonathan V. Dietz: University of Nebraska-Lincoln
Javier Seravalli: University of Nebraska-Lincoln
Oleh Khalimonchuk: University of Nebraska-Lincoln
Antoni Barrientos: University of Miami Miller School of Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-17

Abstract: Abstract Mitochondrial cytochrome c oxidase (CcO) or respiratory chain complex IV is a heme aa3-copper oxygen reductase containing metal centers essential for holo-complex biogenesis and enzymatic function that are assembled by subunit-specific metallochaperones. The enzyme has two copper sites located in the catalytic core subunits. The COX1 subunit harbors the CuB site that tightly associates with heme a3 while the COX2 subunit contains the binuclear CuA site. Here, we report that in human cells the CcO copper chaperones form macromolecular assemblies and cooperate with several twin CX9C proteins to control heme a biosynthesis and coordinate copper transfer sequentially to the CuA and CuB sites. These data on CcO illustrate a mechanism that regulates the biogenesis of macromolecular enzymatic assemblies with several catalytic metal redox centers and prevents the accumulation of cytotoxic reactive assembly intermediates.

Date: 2022
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31413-1

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DOI: 10.1038/s41467-022-31413-1

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