| Autor: |
Koebke, Karl J., Kühl, Toni, Lojou, Elisabeth, Demeler, Borries, Schoepp‐Cothenet, Barbara, Iranzo, Olga, Pecoraro, Vincent L., Ivancich, Anabella |
| Předmět: |
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| Zdroj: |
Angewandte Chemie International Edition; 2/19/2021, Vol. 60 Issue 8, p3974-3978, 5p |
| Abstrakt: |
De Novo metalloprotein design assesses the relationship between metal active site architecture and catalytic reactivity. Herein, we use an α‐helical scaffold to control the iron coordination geometry when a heme cofactor is allowed to bind to either histidine or cysteine ligands, within a single artificial protein. Consequently, we uncovered a reversible pH‐induced switch of the heme axial ligation within this simplified scaffold. Characterization of the specific heme coordination modes was done by using UV/Vis and Electron Paramagnetic Resonance spectroscopies. The penta‐ or hexa‐coordinate thiolate heme (9≤pH≤11) and the penta‐coordinate imidazole heme (6≤pH≤8.5) reproduces well the heme ligation in chloroperoxidases or cyt P450 monooxygenases and peroxidases, respectively. The stability of heme coordination upon ferric/ferrous redox cycling is a crucial property of the construct. At basic pHs, the thiolate mini‐heme protein can catalyze O2 reduction when adsorbed onto a pyrolytic graphite electrode. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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