Protein secondary-shell interactions enhance the photoinduced hydrogen production of cobalt protoporphyrin IX
| Autor: | Dayn J. Sommer, Giovanna Ghirlanda, Michael D. Vaughn |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Hydrogen
Protoporphyrins chemistry.chemical_element Molecular Dynamics Simulation Protein Structure Secondary Catalysis chemistry.chemical_compound Catalytic Domain Materials Chemistry Organic chemistry Histidine Hydrogen production Binding Sites biology Myoglobin Metals and Alloys Active site General Chemistry Combinatorial chemistry Recombinant Proteins Surfaces Coatings and Films Electronic Optical and Magnetic Materials Turnover number chemistry Biocatalysis Mutagenesis Site-Directed Ceramics and Composites biology.protein Cobalt |
| Zdroj: | Chem. Commun.. 50:15852-15855 |
| ISSN: | 1364-548X 1359-7345 |
| DOI: | 10.1039/c4cc06700b |
| Popis: | Hydrogen is an attractive fuel with potential for production scalability, provided that inexpensive, efficient molecular catalysts utilizing base metals can be developed for hydrogen production. Here we show for the first time that cobalt myoglobin (CoMyo) catalyzes hydrogen production in mild aerobic conditions with turnover number of 520 over 8 hours. Compared to free Co-protoporphyrin IX, incorporation into the myoglobin scaffold results in a 4-fold increase in photoinduced hydrogen production activity. Engineered variants in which specific histidine resides in proximity of the active site were mutated to alanine result in modulation of the catalytic activity, with the H64A/H97A mutant displaying activity 2.5-fold higher than wild type. Our results demonstrate that protein scaffolds can augment and modulate the intrinsic catalytic activity of molecular hydrogen production catalysts. |
| Databáze: | OpenAIRE |
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