Probing the access of protons to the K pathway in the Paracoccus denitrificans cytochrome c oxidase-Reference-Cited by-同舟云学术

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Probing the access of protons to the K pathway in the Paracoccus denitrificans cytochrome c oxidase

Published:2004-12-16 Issue:2 Volume:272 Page:404-412
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:

Author:

Richter Oliver-M. H.,Dürr Katharina L.,Kannt Aimo,Ludwig Bernd,Scandurra Francesca M.,Giuffrè Alessandro,Sarti Paolo,Hellwig Petra

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2004.04480.x/fullpdf

Reference38 articles.

1. A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus denitrificans;Ludwig;Proc Natl Acad Sci USA,1980

2. The Paracoccus denitrificans cytochrome aa3 has a third subunit;Haltia;Eur J Biochem,1988

3. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans;Iwata;Nature,1995

4. Molecular genetics of the genus Paracoccus- metabolically versatile bacteria with bioenergetic flexibility;Baker;Microbiol Mol Rev,1998

5. Substitution of aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity;Thomas;Biochemistry,1993

Cited by 26 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structural and functional mechanisms of cytochrome c oxidase;Journal of Inorganic Biochemistry;2025-01

2. Proton collecting antenna residues at the K-channel entrance of the redox-coupled proton pump cytochrome c oxidase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2022-09

3. The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors;Angewandte Chemie International Edition;2021-05-06

4. The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors;Angewandte Chemie;2021-05-06

5. The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2018-09

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