Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Splitting of the O-O bond at the heme-copper catalytic site of respiratory oxidases
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Organic Chemistry.
Show others and affiliations
Number of Authors: 6
2017 (English)In: Science Advances, ISSN 0036-8156, E-ISSN 2375-2548, Vol. 3, no 6, e1700279Article in journal (Refereed) Published
Abstract [en]

Heme-copper oxidases catalyze the four-electron reduction of O-2 to H2O at a catalytic site that is composed of a heme group, a copper ion (Cu-B), and a tyrosine residue. Results from earlier experimental studies have shown that the O-O bond is cleaved simultaneously with electron transfer from a low-spin heme (heme a/b), forming a ferryl state (P-R; Fe4+= O2-, Cu-B(2+)-OH-). We show that with the Thermus thermophilus ba(3) oxidase, at low temperature (10 degrees C, pH 7), electron transfer from the low-spin heme b to the catalytic site is faster by a factor of similar to 10 (tau congruent to 11 mu s) than the formation of the P-R ferryl (t. 110 ms), which indicates that O-2 is reduced before the splitting of the O-O bond. Application of density functional theory indicates that the electron acceptor at the catalytic site is a high-energy peroxy state [Fe3+-O--O-(H+)], which is formed before the P-R ferryl. The rates of heme b oxidation and P-R ferryl formation were more similar at pH 10, indicating that the formation of the high-energy peroxy state involves proton transfer within the catalytic site, consistent with theory. The combined experimental and theoretical data suggest a general mechanism for O-2 reduction by heme-copper oxidases.

Place, publisher, year, edition, pages
2017. Vol. 3, no 6, e1700279
National Category
Chemical Sciences
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:su:diva-147192DOI: 10.1126/sciadv.1700279ISI: 000406370700061OAI: oai:DiVA.org:su-147192DiVA: diva2:1142931
Available from: 2017-09-20 Created: 2017-09-20 Last updated: 2017-09-21Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Poiana, FedericaGonska, NathalieBlomberg, Margareta R. A.Ädelroth, PiaBrzezinski, Peter
By organisation
Department of Biochemistry and BiophysicsDepartment of Organic Chemistry
In the same journal
Science Advances
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 1 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf