Abstract
The environment of the Cu(I) ion in the distal ligand group decides the fate of the reduction of O2 by the two analogues 1 and 2 of the heme a3Cu(B) center in cytochrome c oxidase. The fourfold coordination by N in 1 favors the Cu(II) oxidation state and leads to a 4e--4H+ reduction and the formation of H2O under physiological conditions, while with 2 a 2e--2H+ reduction occurs to form the cytotoxic H2O2.
Original language | English |
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Pages (from-to) | 3397-3400 |
Number of pages | 4 |
Journal | Angewandte Chemie - International Edition |
Volume | 37 |
Issue number | 24 |
DOIs | |
Publication status | Published - 4 Jan 1999 |
Externally published | Yes |
Keywords
- Cytochrome c oxidase
- Electrochemistry
- Heme proteins
- N ligands
- O-O activation