PMID- 37915136
OWN - NLM
STAT- MEDLINE
DCOM- 20231129
LR  - 20231204
IS  - 1976-670X (Electronic)
IS  - 1976-6696 (Print)
IS  - 1976-6696 (Linking)
VI  - 56
IP  - 11
DP  - 2023 Nov
TI  - Coordination chemistry of mitochondrial copper metalloenzymes: exploring 
      implications for copper dyshomeostasis in cell death.
PG  - 575-583
AB  - Mitochondria, fundamental cellular organelles that govern energy metabolism, hold 
      a pivotal role in cellular vitality. While consuming dioxygen to produce 
      adenosine triphosphate (ATP), the electron transfer process within mitochondria 
      can engender the formation of reactive oxygen species that exert dual roles in 
      endothelial homeostatic signaling and oxidative stress. In the context of the 
      intricate electron transfer process, several metal ions that include copper, 
      iron, zinc, and manganese serve as crucial cofactors in mitochondrial 
      metalloenzymes to mediate the synthesis of ATP and antioxidant defense. In this 
      mini review, we provide a comprehensive understanding of the coordination 
      chemistry of mitochondrial cuproenzymes. In detail, cytochrome c oxidase (CcO) 
      reduces dioxygen to water coupled with proton pumping to generate an 
      electrochemical gradient, while superoxide dismutase 1 (SOD1) functions in 
      detoxifying superoxide into hydrogen peroxide. With an emphasis on the catalytic 
      reactions of the copper metalloenzymes and insights into their ligand 
      environment, we also outline the metalation process of these enzymes throughout 
      the copper trafficking system. The impairment of copper homeostasis can trigger 
      mitochondrial dysfunction, and potentially lead to the development of 
      copper-related disorders. We describe the current knowledge regarding 
      copper-mediated toxicity mechanisms, thereby shedding light on prospective 
      therapeutic strategies for pathologies intertwined with copper dyshomeostasis. 
      [BMB Reports 2023; 56(11): 575-583].
FAU - Shim, Daeun
AU  - Shim D
AD  - Department of Applied Chemistry, University of Seoul, Seoul 02504, Korea.
FAU - Han, Jiyeon
AU  - Han J
AD  - Department of Applied Chemistry, University of Seoul, Seoul 02504, Korea.
LA  - eng
PT  - News
PT  - Review
PL  - Korea (South)
TA  - BMB Rep
JT  - BMB reports
JID - 101465334
RN  - 789U1901C5 (Copper)
RN  - 0 (Metalloproteins)
RN  - S88TT14065 (Oxygen)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
SB  - IM
MH  - *Copper/metabolism
MH  - Mitochondria/metabolism
MH  - *Metalloproteins/metabolism
MH  - Oxygen/metabolism
MH  - Cell Death
MH  - Adenosine Triphosphate/metabolism
PMC - PMC10689082
COIS- CONFLICTS OF INTEREST The authors have no conflicting interests.
EDAT- 2023/11/02 06:43
MHDA- 2023/11/29 06:42
PMCR- 2023/10/30
CRDT- 2023/11/02 01:22
PHST- 2023/09/02 00:00 [received]
PHST- 2023/11/29 06:42 [medline]
PHST- 2023/11/02 06:43 [pubmed]
PHST- 2023/11/02 01:22 [entrez]
PHST- 2023/10/30 00:00 [pmc-release]
AID - 6058 [pii]
AID - bmb-56-11-575 [pii]
AID - 10.5483/BMBRep.2023-0172 [doi]
PST - ppublish
SO  - BMB Rep. 2023 Nov;56(11):575-583. doi: 10.5483/BMBRep.2023-0172.