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FEBS Lett. 2013 Mar 18;587(6):770-4. doi: 10.1016/j.febslet.2013.01.069. Epub 2013 Feb 8.

The heme-copper oxidase superfamily shares a Zn2+-binding motif at the entrance to a proton pathway.

Author information

1
Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-106 91 Stockholm, Sweden.

Abstract

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 Zn(2+) inhibit O2-reduction very similarly in C-type as in A-type HCuOs, and furthermore that the binding site shares the same Glu-His motif.

PMID:
23399935
DOI:
10.1016/j.febslet.2013.01.069
[Indexed for MEDLINE]
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