Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase. - sprookjes - yvandenbroek - TriplyDB

Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase.

Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase.

http://www.wikidata.org/entity/Q34789063

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Energy transduction: proton transfer through the respiratory complexes The proton pumping pathway of bovine heart cytochrome c oxidase Proton-pumping mechanism of cytochrome c oxidase: a kinetic master-equation approach Multiscale simulations reveal key features of the proton-pumping mechanism in cytochrome c oxidase Rapid Electron Transfer within the III-IV Supercomplex in Corynebacterium glutamicum.Exploring pathways and barriers for coupled ET/PT in cytochrome c oxidase: a general framework for examining energetics and mechanistic alternatives.Exploration of the cytochrome c oxidase pathway puzzle and examination of the origin of elusive mutational effects.Cytochrome c oxidase: exciting progress and remaining mysteries.Partial steps of charge translocation in the nonpumping N139L mutant of Rhodobacter sphaeroides cytochrome c oxidase with a blocked D-channel.Decoupling 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.Controlled uncoupling and recoupling of proton pumping in cytochrome c oxidase Intricate role of water in proton transport through cytochrome c oxidase.Alternative initial proton acceptors for the D pathway of Rhodobacter sphaeroides cytochrome c oxidase.Impaired proton pumping in cytochrome c oxidase upon structural alteration of the D pathway.Structural elements involved in electron-coupled proton transfer in cytochrome c oxidase.Kinetic models of redox-coupled proton pumping Glutamic acid 242 is a valve in the proton pump of cytochrome c oxidase.Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump.Storage of an excess proton in the hydrogen-bonded network of the d-pathway of cytochrome C oxidase: identification of a protonated water cluster.Direct measurement of proton release by cytochrome c oxidase in solution during the F-->O transition One heme, diverse functions: using biosynthetic myoglobin models to gain insights into heme-copper oxidases and nitric oxide reductases.Kinetic gating of the proton pump in cytochrome c oxidase.Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump.B3LYP study on reduction mechanisms from O2 to H2O at the catalytic sites of fully reduced and mixed-valence bovine cytochrome c oxidases.Structural Changes and Proton Transfer in Cytochrome c Oxidase.Role of the -PEWY-glutamate in catalysis at the Q(o)-site of the Cyt bc(1) complex.Toward a chemical mechanism of proton pumping by the B-type cytochrome c oxidases: application of density functional theory to cytochrome ba3 of Thermus thermophilus.Proton-transport mechanisms in cytochrome c oxidase revealed by studies of kinetic isotope effects.A pathogenic mutation in cytochrome c oxidase results in impaired proton pumping while retaining O(2)-reduction activity.Mutagenesis of tyrosine residues within helix VII in subunit I of the cytochrome cbb₃ oxidase from Rhodobacter capsulatus.Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochrome c oxidase.Spotlight on... Peter Brzezinski. Interview by Tine Walma.

P2860

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P2860

Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase.

http://www.wikidata.org/entity/Q34789063

description

2003 nî lūn-bûn

@nan

2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

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Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

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Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

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Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

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Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

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Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

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Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

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Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

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Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

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PNAS.2432106100

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Proceedings of the National Academy of Sciences of the United States of America

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Redox-coupled proton transloca ...... tling in cytochrome c oxidase.

@en

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Andreas Namslauer

http://www.w3.org/2001/XMLSchema#string

Ashtamurthy S Pawate

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Robert B Gennis

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P2860

The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site

The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides

The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A

VMD: visual molecular dynamics

Influence of structure, pH and membrane potential on proton movement in cytochrome oxidase.

C-terminal truncation and histidine-tagging of cytochrome c oxidase subunit II reveals the native processing site, shows involvement of the C-terminus in cytochrome c binding, and improves the assay for proton pumping.

Single-electron reduction of the oxidized state is coupled to proton uptake via the K pathway in Paracoccus denitrificans cytochrome c oxidase

Proton pumping by cytochrome oxidase: progress, problems and postulates.

Where is 'outside' in cytochrome c oxidase and how and when do protons get there?

The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases.

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15543-15547

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scholarly article

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10.1073/PNAS.2432106100

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26

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100

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Peter Brzezinski

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2003-12-15T00:00:00Z

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8959441

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14676323

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307604

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