ArticleProceedings of the National Academy of Sciences of the United States of America2015
Proton-coupled electron transfer and the role of water molecules in proton pumping by cytochrome c oxidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 68 citations in OpenAlex.
- Surveying Enzyme Crystal Structures Reveals the Commonality of Active-Site Solvent Accessibility and Enzymatic Water Networks.ACS omega · 2025Article
- Molecular switching by proton-coupled electron transport drives giant negative differential resistance.Nature communications · 2024Article
- The critical role of a conserved lysine residue in periplasmic nitrate reductase catalyzed reactions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Protonation-State Dependence of Hydration and Interactions in the Two Proton-Conducting Channels of Cytochrome c Oxidase.International journal of molecular sciences · 2023Article
- Electric fields control water-gated proton transfer in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Quinone binding in respiratory complex I: Going through the eye of a needle. The squeeze-in mechanism of passing the narrow entrance of the quinone site.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Electron Transfer Coupled to Conformational Dynamics in Cell Respiration.Frontiers in molecular biosciences · 2021Article
- Human Mitochondrial Pathologies of the Respiratory Chain and ATP Synthase: Contributions from Studies ofLife (Basel, Switzerland) · 2020Review
- Geometric and Electronic Structure Contributions to O-O Cleavage and the Resultant Intermediate Generated in Heme-Copper Oxidases.Journal of the American Chemical Society · 2019Article
- A low-potential terminal oxidase associated with the iron-only nitrogenase from the nitrogen-fixing bacteriumThe Journal of biological chemistry · 2019Article
- Electric field modulated redox-driven protonation and hydration energetics in energy converting enzymes.Chemical communications (Cambridge, England) · 2019Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Tyrosine-Rich Peptides as a Platform for Assembly and Material Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Review
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- Redox-Driven Proton Pumps of the Respiratory Chain.Biophysical journal · 2018Article
- Dewetting transitions coupled to K-channel activation in cytochromeChemical science · 2018Article
- Oxygen Activation and Energy Conservation by Cytochrome c Oxidase.Chemical reviews · 2018Review
- Insights into functions of the H channel of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Cavity hydration dynamics in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Testing for the Occurrence of Selective Episodes During the Divergence of Otophysan Fishes: Insights from Mitogenomics.Journal of molecular evolution · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular oxygen acts as the terminal electron sink in the respiratory chains of aerobic organisms. Cytochrome c oxidase in the inner membrane of mitochondria and the plasma membrane of bacteria catalyzes the reduction of oxygen to water, and couples the free energy of the reaction to proton pumping across the membrane. The proton-pumping activity contributes to the proton electrochemical gradient, which drives the synthesis of ATP. Based on kinetic experiments on the O-O bond splitting transition of the catalytic cycle (A → P(R)), it has been proposed that the electron transfer to the binuclear iron-copper center of O2 reduction initiates the proton pump mechanism. This key electron transfer event is coupled to an internal proton transfer from a conserved glutamic acid to the proton-loading site of the pump. However, the proton may instead be transferred to the binuclear center to complete the oxygen reduction chemistry, which would constitute a short-circuit. Based on atomistic molecular dynamics simulations of cytochrome c oxidase in an explicit membrane-solvent environment, complemented by related free-energy calculations, we propose that this short-circuit is effectively prevented by a redox-state-dependent organization of water molecules within the protein structure that gates the proton transfer pathway.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.