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Rational Heme Protein Design: All Roads Lead to Rome
Author(s) -
Lin YingWu,
Sawyer Elizabeth B.,
Wang Jiangyun
Publication year - 2013
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201300291
Subject(s) - heme , rational design , hemeprotein , protein design , chemistry , metalloprotein , protein engineering , reactivity (psychology) , combinatorial chemistry , biochemistry , protein structure , enzyme , nanotechnology , materials science , medicine , alternative medicine , pathology
Heme proteins are among the most abundant and important metalloproteins, exerting diverse biological functions including oxygen transport, small molecule sensing, selective CH 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.