Effects of ROS pathway inhibitors and NADH and FADH2 linked substrates on mitochondrial bioenergetics and ROS emission in the heart and kidney cortex and outer medulla

Sadri, Shima; Tomar, Namrata; Yang, Chun; Audi, Said H.; Cowley, Allen W.; Dash, Ranjan K.

doi:10.1016/j.abb.2023.109690

Cited by 4 publications

(2 citation statements)

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“…•OH species can damage mitochondrial DNA, as well as prompt carcinogenesis, apoptosis, and necrosis through nucleosome-driven fragmentation, hindering chromatin-related gene transcription regulation ( 47 , 48 ). SOD as a detoxifying enzyme could maintain the cellular redox balance, protecting cells from oxidative damage ( 49 ). The antioxidant SOD family classified as SOD1, SOD2, and SOD3 plays a crucial role in converting O 2 •− into O 2 and H 2 O 2 , thereby preventing the formation of more reactive ROS, such as •OH ( 49 ).…”

Section: Mitochondrial Sod1mentioning

confidence: 99%

“…SOD as a detoxifying enzyme could maintain the cellular redox balance, protecting cells from oxidative damage ( 49 ). The antioxidant SOD family classified as SOD1, SOD2, and SOD3 plays a crucial role in converting O 2 •− into O 2 and H 2 O 2 , thereby preventing the formation of more reactive ROS, such as •OH ( 49 ). Among them, Cu(I/II)- and Zn(II)-containing SOD1 is primarily localized in the cytoplasm, but a fraction of it has also been identified in the intermembrane space of mitochondria ( 50 ), which will be further discussed in this review.…”

Section: Mitochondrial Sod1mentioning

confidence: 99%

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Coordination chemistry of mitochondrial copper metalloenzymes: exploring implications for copper dyshomeostasis in cell death

Shim,

Han

2023

BMB Rep

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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 (C c O) 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.

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