Abstract
The last decades have seen an increased interest in finding alternative means to produce renewable fuels in order to satisfy the growing energy demands and to minimize environmental impact. Nature can serve as an inspiration for development of these methodologies, as enzymes are able to carry out a wide variety of redox processes at high efficiency, employing a wide array of earth-abundant transition metals to do so. While it is well recognized that the protein environment plays an important role in tuning the properties of the different metal centers, the structure/function relationships between amino acids and catalytic centers are not well resolved. One specific approach to study the role of proteins in both electron and proton transfer is the biomimetic design of redox active peptides, binding organometallic clusters in well-understood protein environments. Here we discuss different strategies for the design of peptides incorporating redox active FeS clusters, [FeFe]-hydrogenase organometallic mimics, and porphyrin centers into different peptide and protein environments in order to understand natural redox enzymes.
| Original language | English |
|---|---|
| Title of host publication | Methods in Enzymology |
| Publisher | Academic Press Inc. |
| Pages | 389-416 |
| Number of pages | 28 |
| Volume | 580 |
| DOIs | |
| Publication status | Published - 2016 |
Publication series
| Name | Methods in Enzymology |
|---|---|
| Volume | 580 |
| ISSN (Print) | 00766879 |
| ISSN (Electronic) | 15577988 |
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Keywords
- Artificial enzymes
- Artificial hydrogenases
- Carbon dioxide reduction
- De novo design
- Hydrogen production
- Iron–sulfur clusters
- Metalloproteins
- Porphyrin-binding proteins
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
Cite this
Design Strategies for Redox Active Metalloenzymes : Applications in Hydrogen Production. / Alcala-Torano, R.; Sommer, D. J.; Bahrami Dizicheh, Z.; Ghirlanda, Giovanna.
Methods in Enzymology. Vol. 580 Academic Press Inc., 2016. p. 389-416 (Methods in Enzymology; Vol. 580).Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Design Strategies for Redox Active Metalloenzymes
T2 - Applications in Hydrogen Production
AU - Alcala-Torano, R.
AU - Sommer, D. J.
AU - Bahrami Dizicheh, Z.
AU - Ghirlanda, Giovanna
PY - 2016
Y1 - 2016
N2 - The last decades have seen an increased interest in finding alternative means to produce renewable fuels in order to satisfy the growing energy demands and to minimize environmental impact. Nature can serve as an inspiration for development of these methodologies, as enzymes are able to carry out a wide variety of redox processes at high efficiency, employing a wide array of earth-abundant transition metals to do so. While it is well recognized that the protein environment plays an important role in tuning the properties of the different metal centers, the structure/function relationships between amino acids and catalytic centers are not well resolved. One specific approach to study the role of proteins in both electron and proton transfer is the biomimetic design of redox active peptides, binding organometallic clusters in well-understood protein environments. Here we discuss different strategies for the design of peptides incorporating redox active FeS clusters, [FeFe]-hydrogenase organometallic mimics, and porphyrin centers into different peptide and protein environments in order to understand natural redox enzymes.
AB - The last decades have seen an increased interest in finding alternative means to produce renewable fuels in order to satisfy the growing energy demands and to minimize environmental impact. Nature can serve as an inspiration for development of these methodologies, as enzymes are able to carry out a wide variety of redox processes at high efficiency, employing a wide array of earth-abundant transition metals to do so. While it is well recognized that the protein environment plays an important role in tuning the properties of the different metal centers, the structure/function relationships between amino acids and catalytic centers are not well resolved. One specific approach to study the role of proteins in both electron and proton transfer is the biomimetic design of redox active peptides, binding organometallic clusters in well-understood protein environments. Here we discuss different strategies for the design of peptides incorporating redox active FeS clusters, [FeFe]-hydrogenase organometallic mimics, and porphyrin centers into different peptide and protein environments in order to understand natural redox enzymes.
KW - Artificial enzymes
KW - Artificial hydrogenases
KW - Carbon dioxide reduction
KW - De novo design
KW - Hydrogen production
KW - Iron–sulfur clusters
KW - Metalloproteins
KW - Porphyrin-binding proteins
UR - http://www.scopus.com/inward/record.url?scp=84984653703&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84984653703&partnerID=8YFLogxK
U2 - 10.1016/bs.mie.2016.06.001
DO - 10.1016/bs.mie.2016.06.001
M3 - Chapter
VL - 580
T3 - Methods in Enzymology
SP - 389
EP - 416
BT - Methods in Enzymology
PB - Academic Press Inc.
ER -