Abstract
Metalloproteins catalyze numerous biological reactions ranging from photosynthesis, respiration, nitrogen fixation to signal transduction and complex chemical reactions. It is thus not surprising that metalloproteins account for almost one-half of the total number of proteins in nature. A considerable effort has been directed toward understanding the structure-function relationships using native proteins. However, it is an ultimate challenge to design metalloproteins using only the minimal features required to reproduce their functionalities as well as confer them with novel and unprecedented functionalities learned from the design process. In this chapter, we review some recent successes in the field of metalloprotein design using either de novo designed or native protein scaffolds. Furthermore, metalloprotein design employing unnatural amino acids or non-native cofactor are summarized. Finally, methodologies employing rational design, combinatorial selection, or both methods are also discussed.
| Original language | English |
|---|---|
| Title of host publication | Bioinorganic Fundamentals and Applications |
| Subtitle of host publication | Metals in Natural Living Systems and Metals in Toxicology and Medicine |
| Publisher | Elsevier Ltd. |
| Pages | 565-593 |
| Number of pages | 29 |
| Volume | 3 |
| ISBN (Print) | 9780080965291 |
| DOIs | |
| Publication status | Published - Aug 2013 |
| Externally published | Yes |
Keywords
- Coiled coils
- Combinatorial protein design
- Cupredoxins
- De novo design
- Electron transfer
- Expressed protein ligation
- Helical bundles
- Heme protein
- Heme-copper oxidase
- Myoglobin
- Native chemical ligation
- Nitric oxide reductase
- Non-native cofactors
- Redesign of proteins
- Unnatural amino acids
- Zinc metalloproteins