Abstract
The active sites of several bioenergetically important metalloenzymes that perform multielectron redox reactions feature heterobimetallic complexes. Herein, we review recent understanding of the structure and mechanisms of hydrogenases, formate dehydrogenases, and carbon monoxide dehydrogenases. Then we evaluate progress toward creating functional, small-molecule complexes that reproduce the activities of these active sites. Particular emphasis is placed on comparing catalytic properties including turnover number, turnover frequency, required overpotential, and catalyst stability. Opportunities and challenges for future work are also considered.
| Original language | English |
|---|---|
| Title of host publication | Topics in Organometallic Chemistry |
| Publisher | Springer Verlag |
| Pages | 233-272 |
| Number of pages | 40 |
| Volume | 59 |
| DOIs | |
| Publication status | Published - Sep 16 2015 |
Publication series
| Name | Topics in Organometallic Chemistry |
|---|---|
| Volume | 59 |
| ISSN (Print) | 14366002 |
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Keywords
- Bio-inspired metallocomplexes
- Biomimicry
- Carbon monoxide dehydrogenase
- Catalysis
- Energy
- Formate dehydrogenase
- Hydrogenase
ASJC Scopus subject areas
- Organic Chemistry
- Inorganic Chemistry
- Catalysis
Cite this
Biomimetic complexes for production of dihydrogen and reduction of CO2 . / Gan, Lu; Jennings, David; Laureanti, Joseph; Jones, Anne Katherine.
Topics in Organometallic Chemistry. Vol. 59 Springer Verlag, 2015. p. 233-272 (Topics in Organometallic Chemistry; Vol. 59).Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Biomimetic complexes for production of dihydrogen and reduction of CO2
AU - Gan, Lu
AU - Jennings, David
AU - Laureanti, Joseph
AU - Jones, Anne Katherine
PY - 2015/9/16
Y1 - 2015/9/16
N2 - The active sites of several bioenergetically important metalloenzymes that perform multielectron redox reactions feature heterobimetallic complexes. Herein, we review recent understanding of the structure and mechanisms of hydrogenases, formate dehydrogenases, and carbon monoxide dehydrogenases. Then we evaluate progress toward creating functional, small-molecule complexes that reproduce the activities of these active sites. Particular emphasis is placed on comparing catalytic properties including turnover number, turnover frequency, required overpotential, and catalyst stability. Opportunities and challenges for future work are also considered.
AB - The active sites of several bioenergetically important metalloenzymes that perform multielectron redox reactions feature heterobimetallic complexes. Herein, we review recent understanding of the structure and mechanisms of hydrogenases, formate dehydrogenases, and carbon monoxide dehydrogenases. Then we evaluate progress toward creating functional, small-molecule complexes that reproduce the activities of these active sites. Particular emphasis is placed on comparing catalytic properties including turnover number, turnover frequency, required overpotential, and catalyst stability. Opportunities and challenges for future work are also considered.
KW - Bio-inspired metallocomplexes
KW - Biomimicry
KW - Carbon monoxide dehydrogenase
KW - Catalysis
KW - Energy
KW - Formate dehydrogenase
KW - Hydrogenase
UR - http://www.scopus.com/inward/record.url?scp=84979243487&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84979243487&partnerID=8YFLogxK
U2 - 10.1007/3418_2015_146
DO - 10.1007/3418_2015_146
M3 - Chapter
AN - SCOPUS:84979243487
VL - 59
T3 - Topics in Organometallic Chemistry
SP - 233
EP - 272
BT - Topics in Organometallic Chemistry
PB - Springer Verlag
ER -