Abstract
This chapter discusses several studies from various classes of metalloenzymes, in which a functional property of the protein, such as electron transfer or catalysis, was either predictably improved or completely altered, or cases where new functionality was engineered into a protein scaffold by modifying the protein cage, as opposed to the catalytic site itself. The chapter focuses on inorganic chemistry, special emphasis is given to metalloenzymes and, where available, the methods used in each study in order to serve as a guide for future studies in metalloenzyme design and engineering. The recent progress in rational design of protein cages for alternative enzymatic functions, and in particular, studies that have strived to predictably alter or impart new functionality to metalloenzymes, have led to important advances in our knowledge of how metalloenzymes work and have set the groundwork for producing designer proteins with a selected function and high rates of catalysis.
| Original language | English (US) |
|---|---|
| Title of host publication | Coordination Chemistry in Protein Cages |
| Subtitle of host publication | Principles, Design, and Applications |
| Publisher | John Wiley and Sons |
| Pages | 111-147 |
| Number of pages | 37 |
| ISBN (Print) | 9781118078570 |
| DOIs | |
| State | Published - Apr 2 2013 |
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Keywords
- Alternative enzymatic functions
- Cupredoxin proteins
- Heme-based enzymes
- Metalloenzyme
- Protein cage
ASJC Scopus subject areas
- Chemistry(all)
Cite this
Rational Design of Protein Cages for Alternative Enzymatic Functions. / Marshall, Nicholas M.; Miner, Kyle D.; Wilson, Tiffany D.; Lu, Yi.
Coordination Chemistry in Protein Cages: Principles, Design, and Applications. John Wiley and Sons, 2013. p. 111-147.Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Rational Design of Protein Cages for Alternative Enzymatic Functions
AU - Marshall, Nicholas M.
AU - Miner, Kyle D.
AU - Wilson, Tiffany D.
AU - Lu, Yi
PY - 2013/4/2
Y1 - 2013/4/2
N2 - This chapter discusses several studies from various classes of metalloenzymes, in which a functional property of the protein, such as electron transfer or catalysis, was either predictably improved or completely altered, or cases where new functionality was engineered into a protein scaffold by modifying the protein cage, as opposed to the catalytic site itself. The chapter focuses on inorganic chemistry, special emphasis is given to metalloenzymes and, where available, the methods used in each study in order to serve as a guide for future studies in metalloenzyme design and engineering. The recent progress in rational design of protein cages for alternative enzymatic functions, and in particular, studies that have strived to predictably alter or impart new functionality to metalloenzymes, have led to important advances in our knowledge of how metalloenzymes work and have set the groundwork for producing designer proteins with a selected function and high rates of catalysis.
AB - This chapter discusses several studies from various classes of metalloenzymes, in which a functional property of the protein, such as electron transfer or catalysis, was either predictably improved or completely altered, or cases where new functionality was engineered into a protein scaffold by modifying the protein cage, as opposed to the catalytic site itself. The chapter focuses on inorganic chemistry, special emphasis is given to metalloenzymes and, where available, the methods used in each study in order to serve as a guide for future studies in metalloenzyme design and engineering. The recent progress in rational design of protein cages for alternative enzymatic functions, and in particular, studies that have strived to predictably alter or impart new functionality to metalloenzymes, have led to important advances in our knowledge of how metalloenzymes work and have set the groundwork for producing designer proteins with a selected function and high rates of catalysis.
KW - Alternative enzymatic functions
KW - Cupredoxin proteins
KW - Heme-based enzymes
KW - Metalloenzyme
KW - Protein cage
UR - http://www.scopus.com/inward/record.url?scp=84887256186&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84887256186&partnerID=8YFLogxK
U2 - 10.1002/9781118571811.ch5
DO - 10.1002/9781118571811.ch5
M3 - Chapter
AN - SCOPUS:84887256186
SN - 9781118078570
SP - 111
EP - 147
BT - Coordination Chemistry in Protein Cages
PB - John Wiley and Sons
ER -