5 publications
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Albumin as a Promiscuous Biocatalyst in Organic Synthesis
Review -
RSC Adv. 2015, 5, 10588-10598, 10.1039/C4RA11206G
Albumin emerged as a biocatalyst in 1980 and the continuing interest in this protein is proved by numerous papers.
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Asymmetric Catalytic Sulfoxidation by a Novel VIV8 Cluster Catalyst in the Presence of Serum Albumin: A Simple and Green Oxidation System
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RSC Adv. 2016, 6, 44154-44162, 10.1039/C6RA08153C
Enantioselective oxidation of a series of alkyl aryl sulfides catalyzed by a novel VIV8 cluster is tested in an aqueous medium in the presence of serum albumin. The procedure is simple, environmentally friendly, selective, and highly reactive.
Metal: VHost protein: Bovine serum albumin (BSA)Anchoring strategy: UndefinedOptimization: ChemicalNotes: Screening with different serum albumins.
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Enabling Protein-Hosted Organocatalytic Transformations
Review -
RSC Adv. 2020, 10, 16147-16161, 10.1039/d0ra01526a
In this review, the development of organocatalytic artificial enzymes will be discussed. This area of protein engineering research has underlying importance, as it enhances the biocompatibility of organocatalysis for applications in chemical and synthetic biology research whilst expanding the catalytic repertoire of enzymes. The approaches towards the preparation of organocatalytic artificial enzymes, techniques used to improve their performance (selectivity and reactivity) as well as examples of their applications are presented. Challenges and opportunities are also discussed.
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Highly Malleable Harm-Binding Site of the Haemoprotein HasA Permits Stable Accommodation of Bulky Tetraphenylporphycenes
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RSC Adv. 2019, 9, 18697-18702, 10.1039/c9ra02872b
Iron(III)- and cobalt(III)-9,10,19,20-tetraphenylporphycenes, which possess bulky phenyl groups at the four meso positions of porphycene, were successfully incorporated into the haem acquisition protein HasA secreted by Pseudomonas aeruginosa. Crystal structure analysis revealed that loops surrounding the haem-binding site are highly flexible, remodelling themselves to accommodate bulky metal complexes with significantly different structures from the native haem cofactor.
Ligand type: PorphyceneHost protein: HasAAnchoring strategy: DativeOptimization: Chemical & geneticReaction: ---Max TON: ---ee: ---PDB: ---Notes: ---
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Metal Incorporated Horseradish Peroxidase (HRP) Catalyzed Oxidation of Resveratrol: Selective Dimerization or Decomposition
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RSC Adv. 2013, 3, 22976, 10.1039/c3ra43784a
Horseradish Peroxidase (HRP) is a commercially available and prevalently used peroxidase with no specific substrate binding domain. However, after being incorporated with different metal cations, new catalytic functions were found in biomimetic oxidation of resveratrol. Based on the results of screening, Ca, Cu, Fe and Mn incorporated enzymes showed distinctive effects, either decomposition or dimerization products were observed.
