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Review
. 2013 Aug 14;113(8):6621-58.
doi: 10.1021/cr300463y. Epub 2013 Jun 14.

Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixation

Aaron M Appel  1 , John E Bercaw, Andrew B Bocarsly, Holger Dobbek, Daniel L DuBois, Michel Dupuis, James G Ferry, Etsuko Fujita, Russ Hille, Paul J A Kenis, Cheryl A Kerfeld, Robert H Morris, Charles H F Peden, Archie R Portis, Stephen W Ragsdale, Thomas B Rauchfuss, Joost N H Reek, Lance C Seefeldt, Rudolf K Thauer, Grover L Waldrop
Affiliations
Review

Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixation

Aaron M Appel et al. Chem Rev. .
No abstract available

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Conflict of interest statement

The authors declare no competing financial interest.

Figures

Figure 1
Figure 1
Structure of the active site of the [FeFe] hydrogenase with simplified depiction of the associated connectivity for electron, hydrogen, and proton transport.
Figure 2
Figure 2
Wave function iso-probability contours for the highest occupied molecular orbital (HOMO) (left side panel) and lowest unoccupied molecular orbital (LUMO) (right side panel) of bent CO2. The surfaces illustrate the strong charge localization associated with these frontier orbitals.
Figure 3
Figure 3
Ball-and-stick drawing of the active site of [NiFe] CO dehydrogenase.
Figure 4
Figure 4
Comparison of the energy efficiencies and current densities for CO2 reduction to formic acid, syngas (CO + H2), and hydrocarbons (methane and ethylene) reported in the literature with those of water electrolyzers. Efficiencies of electrolyzers are total system efficiencies, while the CO2 conversion efficiencies only include cathode losses and neglect anode and system losses.
Figure 5
Figure 5
Left: Structure of EMIM+BF4− ion pair. Right: Schematic of the proposed cocatalytic mechanism in the reduction of CO2 to CO via a complex between the EMIM+ and the CO2·− radical on the surface of the cathode.
Figure 6
Figure 6
Structure of FeMo-cofactor in nitrogenase.
Figure 7
Figure 7
First and second coordination spheres of ACS and hydroformylation catalyst. Left: The A cluster and the cage of hydrophobic residues near the proximal Ni ion surrounding the gas molecule (a Xe atom in the crystal structure). Based on PDB 2A8Y. Right: A rhodium tricarbonyl tripyridylphosphine hydrido complex (HRh(CO)3(PAr3)) embedded in a supramolecular cage formed by a self-assembly of zinc(II) porphyrins around the tripyridylphosphine template.
Figure 8
Figure 8
Structure of the active site of RuBisCO complexed with 2-carboxyarabinitol-1,5-bisphosphate. Based on PDB 1UZD.
Figure 9
Figure 9
Schematic of a cyanobacterial cell illustrating the carbon concentrating mechanism. Shown in the cell is a single carboxysome. Relevant enzymes and metabolites that cross the cell membrane and carboxysome shell are shown. Reactions related to photorespiration catalyzed by RuBisCO in the presence of oxygen are shown in dashed lines. Adapted from Kinney et al.
Figure 10
Figure 10
Partial structure of the CO2 adduct of the MOF Ni2(dobdc). Green, gray, and red spheres represent Ni, C, and O atoms, respectively.
Scheme 1
Scheme 1. Proposed Mechanism for the Reduction of CO2 to CO by [NiFe] CODH
Scheme 2
Scheme 2. Proposed Mechanism for the Reduction of CO2 to CO Catalyzed by [Pd(triphosphine)(solvent)]2+ Complexes
Scheme 3
Scheme 3. Proposed Mechanisms for the Oxidation of CO to CO2 by [MoCu] CODHa
aA: Mechanism implicated by the structure of the n-BuNC-inhibited enzyme. B: Mechanism involving CO coordination to Cu and attack of Mo–O(H) on C atom of carbonyl.
Scheme 4
Scheme 4. Proposed Mechanism for Electrocatalytic Reduction of CO2 to HCOO− by Ir(PCP)H2 (R = t-Bu, L = MeCN)
Scheme 5
Scheme 5. Proposed Mechanism for the Reduction of CO2 to CO by cis-[Ru(bipy)2(CO)H]+
Scheme 6
Scheme 6. Proposed Mechanism for Reduction of CO2 to HCOO− by Selenium- and Molybdenum-Dependent Formate Dehydrogenases
Scheme 7
Scheme 7. Proposed Mechanism for Hydrogenation of CO2 to HCOO− by Ir(PNP)H3 (R = i-Pr, t-Bu)
Scheme 8
Scheme 8. Proposed Catalytic Cycle for Formate Production by Ir Complex with Pendant Base in Second Coordination Sphere (Cp* = C5Me5−)a
aThe box represents a vacant coordination site.
Scheme 9
Scheme 9. Three Proposed Pathways for the Copper-Catalyzed Hydrogenation of CO2 to Methanola
aReproduced with permission from ref . Copyright 2013 Elsevier. The prefixes cis or c, trans or t, refer to the conformation of the partially hydrogenated substrate, and mono- and bi- refer to the number of copper centers attached to the substrate, one and two, respectively.
Scheme 10
Scheme 10. Thermodynamic Relationships (298 K) between Reduced C1 Tetrahydropterin Derivativesa
aEnergetics for the methanogenic pathway are shown in green and for the acetogenic pathway in blue. Water and protons are not shown.
Scheme 11
Scheme 11. Proposed Mechanism for Hydrogenation of HCO2Me Using Ru Pincer Complexes
Scheme 12
Scheme 12
Scheme 13
Scheme 13. Comparison of Biological and Chemical Pathways for C–C Bond Formationa
aLeft: Enzymatic mechanism of acetyl-CoA synthesis by the Ni-metalloenzyme ACS. In the CODH/ACS complex, CO2 is reduced by CODH to generate CO, which is channeled to the ACS active site, where it combines with a methyl group and CoA to generate acetyl-CoA. Right: Mechanism of acetic acid synthesis by the Monsanto process, showing only the key steps and fragments at the metal center. It consists of “organo” and a “metallo” cycles, the later having steps similar to those for ACS.
Scheme 14
Scheme 14
Scheme 15
Scheme 15. Proposed Mechanism for the Fixation of CO2 by RuBisCO
Scheme 16
Scheme 16. Proposed Catalytic Cycle for Carbonic Anhydrase
Chart 1
Chart 1
Chart 2
Chart 2
Structures of the Oxidized (21) and Reduced (22) States of the [MoCu]–CODH and a n-Butylisocyanide Inhibited Form (23)
See this image and copyright information in PMC

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