Science China Chemistry

, Volume 57, Issue 3, pp 346–355 | Cite as

Functional tuning and expanding of myoglobin by rational protein design

  • YingWu Lin
  • JiangYun Wang
  • Yi Lu


Rational protein design is a powerful strategy, not only for revealing the structure and function relationship of natural metallo-proteins, but also for creating artificial metalloproteins with improved properties and functions. Myoglobin (Mb), a small heme protein created by nature with diverse functions, has been shown to be an ideal scaffold for rational protein design. The progress reviewed herein includes fine-tuning its native functions of O2 binding and transport, peroxidase activity and nitrite reductase (NIR) activity, and rational expanding its functionalities to peroxygenase, heme-copper oxidase (HCO), nitric oxide reductase (NOR), as well as hydroxylamine reductase. These studies have enhanced our understanding of how metalloproteins work in nature, and provided insights for rational design of functional metalloproteins for practical applications in the future.


metalloproteins heme proteins protein design oxidase reductase 


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Copyright information

© Science China Press and Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.School of Chemistry and Chemical EngineeringUniversity of South ChinaHengyangChina
  2. 2.Laboratory of Noncoding RNA, Institute of BiophysicsChinese Academy of SciencesBeijingChina
  3. 3.Department of ChemistryUniversity of Illinois at Urbana-ChampaignUrbanaUSA

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