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  Interconversions of P and F intermediates of cytochrome c oxidase from Paracoccus denitrificans

von der Hocht, I., van Wonderen, J. H., Hilbers, F., Angerer, H., MacMillan, F., & Michel, H. (2011). Interconversions of P and F intermediates of cytochrome c oxidase from Paracoccus denitrificans. Proceedings of the National Academy of Sciences of the United States of America, 108(10), 3964-3969. doi:10.1073/pnas.1100950108.

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 Creators:
von der Hocht, Iris1, Author           
van Wonderen, Jessica H.2, Author
Hilbers, Florian1, Author           
Angerer, Heike1, Author           
MacMillan, Fraser2, Author
Michel, Hartmut1, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Henry Wellcome Unit for BiologicalElectron Paramagnetic Resonance Spectroscopy, School of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom, ou_persistent22              

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Free keywords: artificial intermediates; catalase activity; electron paramagnetic resonance spectroscopy; optical difference spectroscopy
 Abstract: Cytochrome c oxidase (CcO) is the terminal enzyme of the respiratory chain. This redox-driven proton pump catalyzes the fourelectron reduction of molecular oxygen to water, one of the most fundamental processes in biology. Elucidation of the intermediate structures in the catalytic cycle is crucial for understanding both the mechanism of oxygen reduction and its coupling to proton pumping. Using CcO from Paracoccus denitrificans, we demonstrate that the artificial F state, classically generated by reaction with an excess of hydrogen peroxide, can be converted into a new P state (in contradiction to the conventional direction of the catalytic cycle) by addition of ammonia at pH 9. We suggest that ammonia coordinates directly to CuB in the binuclear active center in this P state and discuss the chemical structures of both oxoferryl intermediates F and P. Our results are compatible with a superoxide bound to CuB in the F state.

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Language(s): eng - English
 Dates: 2011-03-08
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1100950108
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : PNAS
Source Genre: Journal
 Creator(s):
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 108 (10) Sequence Number: - Start / End Page: 3964 - 3969 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230