Biomimetic Complexes for Production of Dihydrogen and Reduction of CO2

Jennings, David; Laureanti, Joseph A.; Jones, Anne K.

doi:10.1007/3418_2015_146

Cited by 7 publications

(8 citation statements)

References 185 publications

(213 reference statements)

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“…All in all, if not directly considered for applications, enzymes serve as inspiration to discover fundamental principles of fast catalysis that can be executed by simple synthetic molecules. In particular, the enzymes that have inspired the development of biomimetic synthetic catalysts for CO 2 reduction are the carbon monoxide dehydrogenases and the formate dehydrogenases [ 18 , 19 ].…”

Section: Co 2 Activation and Reduction By Enzymmentioning

confidence: 99%

“…There are two types of known carbon monoxide dehydrogenase (CODH) enzymes, which are the MoCu-CODHs and the Ni-CODHs, respectively, characterized by different metals (MoCu or Ni) contained in their active sites [ 18 ]. Both enzymes are able to catalyze the oxidation of CO to CO 2 , albeit Ni-CODHs upkeep the process at much higher turnover frequencies ( k cat values: 4 × 10 4 s −1 ) than MoCu-CODHs (100 s −1 ).…”

Section: Carbon Dioxide Reduction Enzymesmentioning

confidence: 99%

“…The mechanism of this class of catalysts, firstly reported by DuBois and coworkers [ 66 , 67 ], has been studied in detail [ 18 , 45 , 49 , 61 , 68 , 69 ].…”

Section: Carbon Dioxide Reduction Mediated By Synthetic Catalystsmentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

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Biomimetic Approach to CO₂ Reduction

Gamba

2018

Bioinorganic Chemistry and Applications

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The development of artificial photosynthetic technologies able to produce solar-fuels from CO2 reduction is a fundamental task that requires the employment of specific catalysts being accomplished. Besides, effective catalysts are also demanded to capture atmospheric CO2, mitigating the effects of its constantly increasing emission. Biomimetic transition metal complexes are considered ideal platforms to develop efficient and selective catalysts to be implemented in electrocatalytic and photocatalytic devices. These catalysts, designed according to the inspiration provided by nature, are simple synthetic molecular systems capable of mimic features of the enzymatic activity. The present review aims to focus the attention on the mechanistic and structural aspects highlighted to be necessary to promote a proper catalytic activity. The determination of these characteristics is of interest both for clarifying aspects of the catalytic cycle of natural enzymes that are still unknown and for developing synthetic molecular catalysts that can readily be applied to artificial photosynthetic devices.

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Section: Co 2 Activation and Reduction By Enzymmentioning

confidence: 99%

Section: Carbon Dioxide Reduction Enzymesmentioning

confidence: 99%

“…The mechanism of this class of catalysts, firstly reported by DuBois and coworkers [ 66 , 67 ], has been studied in detail [ 18 , 45 , 49 , 61 , 68 , 69 ].…”

Section: Carbon Dioxide Reduction Mediated By Synthetic Catalystsmentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

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Biomimetic Approach to CO₂ Reduction

Gamba

2018

Bioinorganic Chemistry and Applications

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“…Because metalloenzymes are very efficient, fast, and selective in the conversion and storage of energy under ambient conditions, they are ideal models upon which to base synthetic mimics able to efficiently interconvert electrical and chemical energy. 6,7 One of the critical features responsible for the high reactivity and specificity of metalloenzymes is the protein scaffold surrounding the metal at the active site. 8,9 Protein scaffolds are composed of elements of secondary structure dominated by αhelices and β-sheets that in turn fold into higher order tertiary structures with a well-defined spatial arrangement of hydrophobic and hydrophilic residues.…”

Section: ■ Introductionmentioning

confidence: 99%

A Positive Charge in the Outer Coordination Sphere of an Artificial Enzyme Increases CO₂ Hydrogenation

et al. 2020

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The protein scaffold around the active site of enzymes is known to influence catalytic activity, but specific scaffold features responsible for favorable influences are often not known. This study focuses on using an artificial metalloenzyme to probe one specific feature of the scaffold, the position of a positive charge in the outer coordination sphere around the active site. Previous work showed that a small molecular complex, [Rh(P Et 2 N glycine P Et 2)2 ] − , immobilized covalently within a protein scaffold was activated for CO 2 hydrogenation. Here, using an iterative design where the effect of arginine, histidine, or lysine residues placed in the outer coordination sphere of the catalytic active site were evaluated, we tested the hypothesis that positively charged groups facilitate CO 2 hydrogenation with seven unique constructs. Single-, double-, and triple-point mutations were introduced to directly compare catalytic activity, as monitored by turnover frequencies (TOFs) measured in real time with 1 H NMR spectroscopy, and evaluate related structural and electronic properties. Two of the seven constructs showed a 2-and 3-fold increase relative to the wild type, with overall rates ranging from 0.2 to 0.7 h −1 , and a crystal structure of the fastest of these shows the positive charge positioned next to the active site. A crystal structure of the arginine-containing complex shows that the arginines are positioned near the metal. Molecular dynamics (MD) studies also suggest that the positive charge is oriented next to the active site in the two constructs with faster rates but not in the others and that the positive charge near the active site holds the CO 2 near the metal, all consistent with a positive charge appropriately positioned in the scaffold benefiting catalysis. The MD studies also suggest that changes in the water distribution around the active site may contribute to catalytic activity, while modest structural changes and movement of the complex within the scaffold do not.

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