PMID- 35750769
OWN - NLM
STAT- MEDLINE
DCOM- 20220628
LR  - 20230417
IS  - 2041-1723 (Electronic)
IS  - 2041-1723 (Linking)
VI  - 13
IP  - 1
DP  - 2022 Jun 24
TI  - Coordination of metal center biogenesis in human cytochrome c oxidase.
PG  - 3615
LID - 10.1038/s41467-022-31413-1 [doi]
LID - 3615
AB  - Mitochondrial cytochrome c oxidase (CcO) or respiratory chain complex IV is a 
      heme aa(3)-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 Cu(B) site that tightly 
      associates with heme a(3) while the COX2 subunit contains the binuclear Cu(A) 
      site. Here, we report that in human cells the CcO copper chaperones form 
      macromolecular assemblies and cooperate with several twin CX(9)C proteins to 
      control heme a biosynthesis and coordinate copper transfer sequentially to the 
      Cu(A) and Cu(B) 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.
CI  - (c) 2022. The Author(s).
FAU - Nyvltova, Eva
AU  - Nyvltova E
AD  - Department of Neurology, University of Miami Miller School of Medicine, 1420NW 
      9th Ave, Miami, FL, 33136, USA.
FAU - Dietz, Jonathan V
AU  - Dietz JV
AD  - Department of Biochemistry, University of Nebraska-Lincoln, 1901 Vine St. Beadle 
      Center, Lincoln, NE, 68588, USA.
FAU - Seravalli, Javier
AU  - Seravalli J
AD  - Nebraska Redox Biology Center, University of Nebraska-Lincoln, 1901 Vine St. 
      Beadle Center, Lincoln, NE, 68588, USA.
FAU - Khalimonchuk, Oleh
AU  - Khalimonchuk O
AUID- ORCID: 0000-0002-3972-8678
AD  - Department of Biochemistry, University of Nebraska-Lincoln, 1901 Vine St. Beadle 
      Center, Lincoln, NE, 68588, USA.
AD  - Nebraska Redox Biology Center, University of Nebraska-Lincoln, 1901 Vine St. 
      Beadle Center, Lincoln, NE, 68588, USA.
FAU - Barrientos, Antoni
AU  - Barrientos A
AUID- ORCID: 0000-0001-9018-3231
AD  - Department of Neurology, University of Miami Miller School of Medicine, 1420NW 
      9th Ave, Miami, FL, 33136, USA. abarrientos@med.miami.edu.
AD  - Department of Biochemistry and Molecular Biology, University of Miami Miller 
      School of Medicine, 1420NW 9th Ave, Miami, FL, 33136, USA. 
      abarrientos@med.miami.edu.
LA  - eng
GR  - R35 GM118141/GM/NIGMS NIH HHS/United States
GR  - R35 GM131701/GM/NIGMS NIH HHS/United States
GR  - T32 GM107001/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20220624
PL  - England
TA  - Nat Commun
JT  - Nature communications
JID - 101528555
RN  - 0 (Molecular Chaperones)
RN  - 42VZT0U6YR (Heme)
RN  - 789U1901C5 (Copper)
RN  - 9007-43-6 (Cytochromes c)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Copper/metabolism
MH  - Cytochromes c/metabolism
MH  - *Electron Transport Complex IV/chemistry/metabolism
MH  - Heme/metabolism
MH  - Humans
MH  - Molecular Chaperones/genetics/metabolism
MH  - *Oxidoreductases/metabolism
PMC - PMC9232578
COIS- The authors declare no competing interests.
EDAT- 2022/06/25 06:00
MHDA- 2022/06/29 06:00
PMCR- 2022/06/24
CRDT- 2022/06/24 23:22
PHST- 2021/06/15 00:00 [received]
PHST- 2022/06/16 00:00 [accepted]
PHST- 2022/06/25 06:00 [pubmed]
PHST- 2022/06/29 06:00 [medline]
PHST- 2022/06/24 23:22 [entrez]
PHST- 2022/06/24 00:00 [pmc-release]
AID - 10.1038/s41467-022-31413-1 [pii]
AID - 31413 [pii]
AID - 10.1038/s41467-022-31413-1 [doi]
PST - epublish
SO  - Nat Commun. 2022 Jun 24;13(1):3615. doi: 10.1038/s41467-022-31413-1.