Rational heme protein design: all roads lead to Rome.

Ying-Wu Lin, Elizabeth B Sawyer, Jiangyun Wang

Journal: Chemistry, an Asian journal 2014;8(11):2534-44

PMID: 23704071

Abstract

Heme proteins are among the most abundant and important metalloproteins, exerting diverse biological functions including oxygen transport, small molecule sensing, selective C-H bond activation, nitrite reduction, and electron transfer. Rational heme protein designs focus on the modification of the heme-binding active site and the heme group, protein hybridization and domain swapping, and de novo design. These strategies not only provide us with unique advantages for illustrating the structure-property-reactivity-function (SPRF) relationship of heme proteins in nature but also endow us with the ability to create novel biocatalysts and biosensors.

Address: School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001 (China).

DOI: 10.1002/asia.201300291

Link outs

Free resources

Other Literature Sources:

https://scite.ai/reports/23704071

Subscription / membership required

Full Text Sources:

https://doi.org/10.1002/asia.201300291

MeSH Terms: Binding Sites, Biocatalysis, Biocompatible Materials, Catalytic Domain, Hemeproteins, Models, Molecular, Recombinant Fusion Proteins