The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases.
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Energy transduction: proton transfer through the respiratory complexesCrystallographic and online spectral evidence for role of conformational change and conserved water in cytochrome oxidase proton pumpSite-directed mutations in the mitochondrially encoded subunits I and III of yeast cytochrome oxidase.Multiscale simulations reveal key features of the proton-pumping mechanism in cytochrome c oxidaseFunctional role of Thr-312 and Thr-315 in the proton-transfer pathway in ba3 Cytochrome c oxidase from Thermus thermophilus.Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations.Exploring pathways and barriers for coupled ET/PT in cytochrome c oxidase: a general framework for examining energetics and mechanistic alternatives.Proton-coupled electron transfer and the role of water molecules in proton pumping by cytochrome c oxidaseNoninvasive auto-photoreduction used as a tool for studying structural changes in heme-copper oxidases by FTIR spectroscopyDecoupling mutations in the D-channel of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that a continuous hydrogen-bonded chain of waters is essential for proton pumping.Blocking the K-pathway still allows rapid one-electron reduction of the binuclear center during the anaerobic reduction of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides.Controlled uncoupling and recoupling of proton pumping in cytochrome c oxidaseTheory of coupled electron and proton transfer reactions.Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase.Alternative initial proton acceptors for the D pathway of Rhodobacter sphaeroides cytochrome c oxidase.Water molecule reorganization in cytochrome c oxidase revealed by FTIR spectroscopy.Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase.Entrance of the proton pathway in cbb3-type heme-copper oxidases.The catalytic cycle of cytochrome c oxidase is not the sum of its two halves.Structural elements involved in electron-coupled proton transfer in cytochrome c oxidase.On the role of the K-proton transfer pathway in cytochrome c oxidase.A mitochondrial DNA mutation linked to colon cancer results in proton leaks in cytochrome c oxidase.Coupled electron and proton transfer reactions during the O→E transition in bovine cytochrome c oxidase.Functions of the hydrophilic channels in protonmotive cytochrome c oxidase.Current advances in research of cytochrome c oxidase.Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature.B3LYP study on reduction mechanisms from O2 to H2O at the catalytic sites of fully reduced and mixed-valence bovine cytochrome c oxidases.Theoretical identification of proton channels in the quinol oxidase aa3 from Acidianus ambivalens.Heme-heme communication during the alkaline-induced structural transition in cytochrome c oxidase.Water exit pathways and proton pumping mechanism in B-type cytochrome c oxidase from molecular dynamics simulations.Calculated proton uptake on anaerobic reduction of cytochrome C oxidase: is the reaction electroneutral?Net proton uptake is preceded by multiple proton transfer steps upon electron injection into cytochrome c oxidase.Proton-transport mechanisms in cytochrome c oxidase revealed by studies of kinetic isotope effects.Elevated proton leak of the intermediate OH in cytochrome c oxidase.Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating.Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochrome c oxidase.Electron transfer processes in subunit I mutants of cytochrome bo quinol oxidase in Escherichia coli.Redox-induced protein structural changes in cytochrome bo revealed by Fourier transform infrared spectroscopy and [13C]Tyr labeling.Influence of glutamic acid residues and pH on the properties of transmembrane helices.The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain.
P2860
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P2860
The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases.
description
2000 nî lūn-bûn
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2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The role of the D- and K-pathw ...... n of the haem-copper oxidases.
@ast
The role of the D- and K-pathw ...... n of the haem-copper oxidases.
@en
The role of the D- and K-pathw ...... n of the haem-copper oxidases.
@nl
type
label
The role of the D- and K-pathw ...... n of the haem-copper oxidases.
@ast
The role of the D- and K-pathw ...... n of the haem-copper oxidases.
@en
The role of the D- and K-pathw ...... n of the haem-copper oxidases.
@nl
prefLabel
The role of the D- and K-pathw ...... n of the haem-copper oxidases.
@ast
The role of the D- and K-pathw ...... n of the haem-copper oxidases.
@en
The role of the D- and K-pathw ...... n of the haem-copper oxidases.
@nl
P2093
P1476
The role of the D- and K-pathw ...... on of the haem-copper oxidases
@en
P2093
A Jasaitis
C Backgren
M I Verkhovsky
M Wikström
P304
P356
10.1016/S0005-2728(00)00191-2
P407
P577
2000-08-01T00:00:00Z