The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction

  • Cytochrome c oxidase catalyzes the reduction of oxygen to water. This process is accompanied by the vectorial transport of protons across the mitochondrial or bacterial membrane (“proton pumping”). The mechanism of proton pumping is still a matter of debate. Many proposed mechanisms require structural changes during the reaction cycle of cytochrome c oxidase. Therefore, the structure of the cytochrome c oxidase was determined in the completely oxidized and in the completely reduced states at a temperature of 100 K. No ligand exchanges or other major structural changes upon reduction of the cytochrome coxidase from Paracoccus denitrificans were observed. The three histidine CuB ligands are well defined in the oxidized and in the reduced states. These results are hardly compatible with the “histidine cycle” mechanisms formulated previously.

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Metadaten
Author:Axel HarrengaGND, Hartmut MichelORCiDGND
URN:urn:nbn:de:hebis:30:3-758640
DOI:https://doi.org/10.1074/jbc.274.47.33296
ISSN:0021-9258
Pubmed Id:https://pubmed.ncbi.nlm.nih.gov/10559205
Parent Title (English):Journal of biological chemistry
Publisher:American Society for Biochemistry and Molecular Biology Publications
Place of publication:Bethesda, Md
Document Type:Article
Language:English
Date of Publication (online):2021/01/04
Year of first Publication:1999
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2023/11/14
Volume:274
Issue:47
Page Number:4
First Page:33296
Last Page:33299
HeBIS-PPN:516504266
Institutes:Biochemie, Chemie und Pharmazie
Angeschlossene und kooperierende Institutionen / MPI für Biophysik
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - CC BY - Namensnennung 4.0 International