Hemin-micelles immobilized in alginate hydrogels as artificial enzymes with peroxidase-like activity and substrate selectivity
- 31 January 2017
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Biomaterials Science
- Vol. 5 (3) , 570-577
Abstract
Hemin-micelles immobilized in hydrogels were designed, which function as efficient artificial enzymes with high catalytic activity and substrate selectivity.Keywords
Funding Information
- National Natural Science Foundation of China (51390483)
- National Natural Science Foundation of China (91527306)
This publication has 50 references indexed in Scilit:
- Highly stretchable and tough hydrogelsNature, 2012
- Reversible ON/OFF Nanoswitch for Organocatalysis: Mimicking the Locking and Unlocking Operation of CaMKIIAngewandte Chemie International Edition, 2012
- Alginate: Properties and biomedical applicationsProgress in Polymer Science, 2012
- Supramolecular enzyme mimics by self-assemblyCurrent Opinion in Colloid & Interface Science, 2011
- Artificial Metalloenzyme for Enantioselective Sulfoxidation Based on Vanadyl-Loaded StreptavidinJournal of the American Chemical Society, 2008
- High Catalytic Activities of Artificial Peroxidases Based on Supramolecular Hydrogels That Contain Heme ModelsChemistry – A European Journal, 2008
- Construction of the Active Site of Glutathione Peroxidase on Polymer-Based NanoparticlesBiomacromolecules, 2008
- Complexes of Horseradish Peroxidase with Formate, Acetate, and Carbon MonoxideBiochemistry, 2004
- The catalytic pathway of horseradish peroxidase at high resolutionNature, 2002
- Self-Assembly at All ScalesScience, 2002