title: Rational heme protein design: all roads lead to Rome.
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.
authors.affiliation: School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001 (China).
authors.forename: Ying-Wu
authors.initials: YW
authors.lastname: Lin
authors.forename: Elizabeth B
authors.initials: EB
authors.lastname: Sawyer
authors.forename: Jiangyun
authors.initials: J
authors.lastname: Wang
mesh_terms: D001665:Binding Sites; D055162:Biocatalysis; D001672:Biocompatible Materials / Q000737:chemistry / Q000378:metabolism; D020134:Catalytic Domain; D006420:Hemeproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics
chemical_list: D001672:Biocompatible Materials; D006420:Hemeproteins; D011993:Recombinant Fusion Proteins
keywords: heme proteins; metalloporphyrin; metalloproteins; protein design; unnatural amino acids