The electrochemical properties of the highly diverse terminal oxidases from different organisms
Abstract
Terminal oxidases are critical for aerobic respiratory chains of prokaryotes and eukaryotes, responsible for the final step in the electron transport chain. These enzymes catalyze the transfer of electrons from reduced electron carriers (such as cytochrome c or quinols) to the terminal electron acceptor, molecular oxygen (O₂), thereby reducing it to water. They play a pivotal role in aerobic respiration and energy metabolism, adapting to diverse environmental and physiological needs across different organisms. This review summarizes the electrochemical properties of terminal oxidases from different organisms and reveals their high degree of adaptivity with redox potentials spanning more than 500 mV. The electrocatalytic response in direct electrochemical approaches is described giving insight into the rich and complex electron and proton transfer catalysed by these essential enzymes. • Terminal oxidases show distinct electrochemical properties depending on their structural and mechanistic properties. • The hemes have redox potentials spanning for more than 500 mV in the different terminal oxidases. • Also cytochrome bd oxidases present distinct electrochemical properties depending on the environment conditions of their host.
Related
- Respire to ripe: The involvement of the mitochondrial alternative oxidases in tomato fruit ripening
- Directed evolution of laccase from Thermus thermophilus HB27 reveals a variant with enhanced high temperature catalytic activity and electrochemical properties
- Effects of Different Vegetation Types on Soil Hydrological Properties, Understory Diversity, and Water Conservation Capacity in the Horqin Sandy Land, China
- Iterative computational bioprospecting of hydroxymethylfurfural oxidases combining molecular simulation and machine learning
- Effect of gelation methods on the gel properties of surimi from marine fish adapted to different thermal environments
BibTeX
@article{hellwig2026electrochemical,
title = {{The electrochemical properties of the highly diverse terminal oxidases from different organisms}},
author = {Petra Hellwig},
journal = {Bioelectrochemistry},
year = {2026},
month = nov,
doi = {10.1016/j.bioelechem.2025.108946},
url = {https://hal.science/hal-05852013v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - The electrochemical properties of the highly diverse terminal oxidases from different organisms
AU - Petra Hellwig
PY - 2026
DA - 2026/11/04
JO - Bioelectrochemistry
DO - 10.1016/j.bioelechem.2025.108946
UR - https://hal.science/hal-05852013v1
AB - Terminal oxidases are critical for aerobic respiratory chains of prokaryotes and eukaryotes, responsible for the final step in the electron transport chain. These enzymes catalyze the transfer of electrons from reduced electron carriers (such as cytochrome c or quinols) to the terminal electron acceptor, molecular oxygen (O₂), thereby reducing it to water. They play a pivotal role in aerobic respiration and energy metabolism, adapting to diverse environmental and physiological needs across different organisms. This review summarizes the electrochemical properties of terminal oxidases from different organisms and reveals their high degree of adaptivity with redox potentials spanning more than 500 mV. The electrocatalytic response in direct electrochemical approaches is described giving insight into the rich and complex electron and proton transfer catalysed by these essential enzymes. • Terminal oxidases show distinct electrochemical properties depending on their structural and mechanistic properties. • The hemes have redox potentials spanning for more than 500 mV in the different terminal oxidases. • Also cytochrome bd oxidases present distinct electrochemical properties depending on the environment conditions of their host.
SN - 1567-5394
ER -