Asp-193 and Glu-218 of subunit II are involved in the Mn 2+-binding of Paracoccus denitrificans cytochrome c oxidase

Cytochrome c oxidase contains a binding site for a non-redox-active metal at the interface of subunits I and II, usually a magnesium ion. In Paracoccus denitrificans oxidase, typically 20% may be replaced by manganese, using standard growth media. Site-directed mutants were constructed in subunit II...

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Bibliographic Details
Published in:FEBS letters 1997-06, Vol.409 (2), p.128-130
Main Authors: Witt, Heike, Wittershagen, Axel, Bill, Eckhard, Kolbesen, B.O, Ludwig, Bernd
Format: Article
Language:English
Subjects:
Electron transfer
Magnesium-binding site
Non-redox-active metal
Terminal oxidase
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Summary:Cytochrome c oxidase contains a binding site for a non-redox-active metal at the interface of subunits I and II, usually a magnesium ion. In Paracoccus denitrificans oxidase, typically 20% may be replaced by manganese, using standard growth media. Site-directed mutants were constructed in subunit II (D193N and E218Q), and the isolated enzymes analyzed by total-reflection X-ray fluorescence spectrometry and EPR. Both mutants show a strong reduction of the manganese stoichiometry and a diminished electron transfer activity, demonstrating that D193 and E218 are involved in the binding of a manganese/magnesium ion in this site.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00485-7