Abstract
A novel homobinuclear Cu2 complex describes best the CuA center of the cytochrome‐c oxidase from bovine heart mitochondria according to EXAFS investigations. In this complex, which contains two terminal histidine residues, two cysteine sulfur bridges, and probably a bridging oxygen donor function, the CuCu distance of 2.46 Å is very short. The structure of the Fea3‐CuB center was likewise determined. (Figure Presented.)
| Original language | English |
|---|---|
| Pages (from-to) | 1488-1492 |
| Number of pages | 5 |
| Journal | Angewandte Chemie - International Edition |
| Volume | 34 |
| Issue number | 13-14 |
| DOIs | |
| Publication status | Published - 31 Jul 1995 |
| Externally published | Yes |
Keywords
- X‐ray absorption spectroscopy
- cytochrome‐c oxidase
- metalloenzymes
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