Artificial Metalloenzymes: Types and advantages over classic metalloenzymes

• Autor: Castañeda, Alvaro
• Formato: artículo
• Fecha de Publicación: 2020
• Institución: Pontificia Universidad Católica del Perú
• Repositorio: Revistas - Pontificia Universidad Católica del Perú
• Lenguaje: español
• OAI Identifier: oai:ojs.pkp.sfu.ca:article/22998
• Enlace del recurso: http://revistas.pucp.edu.pe/index.php/quimica/article/view/22998
• Nivel de acceso: acceso abierto

The development of high yield and high selectivity catalysts has been a topic of great interest since the beginning of the industrial era, as these catalysts can be greatly helpful in synthesis at either laboratory or industrial stages. Lately, the modification of metalloenzymes has acquired quite a lot of attention due to the achievements of recent years, which led to its recognition with the Nobel Prize in Chemistry in 2018. By making a variety of modifications, it is possible to change the enzyme’s substrate as well as the reaction medium in which they are active. These modifications can be made in the amino acid sequence of the protein, in the identity of the active site metal or both. Similarly, it is possible for metalloenzymes and traditional catalysts to work as one, with the objective to vastly improve catalytic efficiency.