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The heme-copper oxidase superfamily shares a Zn2+-binding motif at the entrance to a proton pathway
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2013 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 587, no 6, 770-774 p.Article in journal (Refereed) Published
Abstract [en]

Heme-copper oxidases (HCuOs) catalyse the reduction of oxygen, using the liberated free energy to maintain a proton-motive force across the membrane. In the mitochondrial-like A-type HCuOs, binding of heavy metal ions at the surface of the protein inhibits proton transfer. In bacterial C-type oxidases, the entry point to the proton pathway is on an accessory subunit unrelated to any subunit in A-type HCuOs. Despite this, we show here that heavy metal ions such as Zn2+ inhibit O-2-reduction very similarly in C-type as in A-type HCuOs, and furthermore that the binding site shares the same Glu-His motif. (C) 2013 Federation of European Biochemical Societies.

Place, publisher, year, edition, pages
2013. Vol. 587, no 6, 770-774 p.
Keyword [en]
cbb(3), Proton transfer, K-pathway, Nickel, Liposome, Nitric oxide reductase
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-88996DOI: 10.1016/j.febslet.2013.01.069ISI: 000315947400036OAI: oai:DiVA.org:su-88996DiVA: diva2:615283
Note

AuthorCount:2;

Available from: 2013-04-09 Created: 2013-04-08 Last updated: 2017-12-06Bibliographically approved

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