Construction of a hybrid biocatalyst containing a covalently-linked terpyridine metal complex within a cavity of aponitrobindin

Himiyama, Tomoki; Sauer, Daniel F.; Onoda, Akira; Spaniol, Thomas P.; Okuda, Jun; Hayashi, Takashi

doi:10.1016/j.jinorgbio.2015.12.026

Cited by 36 publications

(35 citation statements)

References 40 publications

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“…The constructed metalloenzyme catalyzes a Diels-Alder reaction between azachalcone and cyclopentadiene in 22% yield. This study suggests that after linking a catalytic motif, the cavity of apo-NB still has sufficient space for simultaneous binding of two substrates, dienophile and diene [149]. In a previous study, Lewis and co-workers complex, which catalyzes oxidation of benzylic methylene groups into carbonyl groups and styrene into phenyl epoxide, respectively, by using peroxyacetic acid as an oxidant.…”

Section: In Apo-nitrobindinmentioning

confidence: 81%

Rational design of metalloenzymes: From single to multiple active sites

Lin

2017

Coordination Chemistry Reviews

137

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Artificial metalloenzymes combine the advantages of both natural enzymes and chemically synthesized models, which have achieved significant progress in the last decade. This review summarizes the recent achievements in rational design of metalloenzymes from single to multiple active sites in natural or de novo protein scaffolds, with a diverse range of functionalities, even beyond those of natural metalloenzymes. These achievements include construction of mononuclear active site by metal substitution or incorporation, design of homo-or hetero-dinuclear site, introduction of Fe-sulfur or other metal clusters, reconstitution of metallo-porphyrins or other metal complexes, and design of dual or multiple active sites in single, dimeric proteins, de novo proteins, protein-protein interfaces, as well as protein oligomers and polymers. Other new trends in recent designs are also discussed. The progress not only elucidates the structural and functional relationship of natural metalloenzymes, but also provides practical clues for design of advanced artificial metalloenzymes with potential applications.

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Section: In Apo-nitrobindinmentioning

confidence: 81%

Rational design of metalloenzymes: From single to multiple active sites

Lin

2017

Coordination Chemistry Reviews

137

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“…364 The TOF of the Diels-Alder reaction between cyclopentadiene and acrolein (a rare example not involving aza-chalcones, Scheme 60 b) was increased more than threefold with the ArM relative to the free cofactor. Kamer 353 and later Okuda and Hayashi 365 have demonstrated that bidentate and tridentate nitrogen ligands (Figure 23, 194-202 Cu(II). 367 High conversion and enantiomeric excess (both > 90%) were observed for the reaction displayed in Scheme 60 a) (…”

Section: Polymerization (Non-romp)mentioning

confidence: 96%

Artificial Metalloenzymes: Reaction Scope and Optimization Strategies

et al. 2017

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The incorporation of a synthetic, catalytically competent metallocofactor into a protein scaffold to generate an artificial metalloenzyme (ArM) has been explored since the late 1970's. Progress in the ensuing years was limited by the tools available for both organometallic synthesis and protein engineering. Advances in both of these areas, combined with increased appreciation of the potential benefits of combining attractive features of both homogeneous catalysis and enzymatic catalysis, led to a resurgence of interest in ArMs starting in the early 2000's. Perhaps the most intriguing of potential ArM properties is their ability to endow homogeneous catalysts with a genetic memory. Indeed, incorporating a homogeneous catalyst into a genetically encoded scaffold offers the opportunity to improve ArM performance by directed evolution. This capability could, in turn, lead to improvements in ArM efficiency similar to those obtained for natural enzymes, providing systems suitable for practical applications and greater insight into the role of second coordination sphere interactions in organometallic catalysis. Since its renaissance in the early 2000's, different aspects of artificial metalloenzymes have been extensively reviewed and highlighted. Our intent is to provide a comprehensive overview of all work in the field up to December 2016, organized according to reaction class. Because of the wide range of non-natural reactions catalyzed by ArMs, this was done using a functional-group transformation classification. The review begins with a summary of the proteins and the anchoring strategies used to date for the creation of ArMs, followed by a historical perspective. Then follows a summary of the reactions catalyzed by ArMs and a concluding critical outlook. This analysis allows for comparison of similar reactions catalyzed by ArMs constructed using different metallocofactor anchoring strategies, cofactors, protein scaffolds, and mutagenesis strategies. These data will be used to construct a searchable Web site on ArMs that will be updated regularly by the authors.

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“…Interestingly, the experiment run with 1,3‐diphenylprop‐2‐en‐1‐one in place of 11 led to only 5 % yield and 56 % ee thus demonstrating the positive influence of the bidentate ligand. This reaction has since been frequently used as a model reaction to evaluate new biohybrid scaffolds in the context of asymmetric Diels‐Alder reactions in water …”

Section: Peptide and Protein‐based Asymmetric Catalysismentioning

confidence: 99%

“…This reaction has since been frequently used as a model reaction to evaluate new biohybrid scaffolds in the context of asymmetric Diels-Alder reactions in water. [36,[92][93][94][95][96][97][98][99]…”

Section: Peptide and Protein-based Asymmetric Catalysismentioning

confidence: 99%

α,β‐Unsaturated 2‐Acyl‐Imidazoles in Asymmetric Biohybrid Catalysis

et al. 2019

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α,β-Unsaturated acylimidazoles have been used in a plethora of enantioselective transformations over the years and have unsurprisingly become privileged building blocks for asymmetric catalysis. Interestingly however, their use in asymmetric biohybrid catalysis as bidentate substrates able to interact with artificial metalloenzymes has only recently emerged, expanding considerably in the last few years. Easy to prepare and to posttransform, α,β-unsaturated acylimidazoles appear as leading synthons for the asymmetric construction of CÀ C and CÀ O bonds. This Minireview highlights the current and increasing interest of these key building blocks in the context of asymmetric biohybrid catalysis with the aim to stimulate further research into their still unexploited potential. The use of these α,β-unsaturated acylimidazoles in metal-catalyzed and organocatalyzed transformations will be covered in a back-to-back Minireview

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Construction of a hybrid biocatalyst containing a covalently-linked terpyridine metal complex within a cavity of aponitrobindin

Cited by 36 publications

References 40 publications

Rational design of metalloenzymes: From single to multiple active sites

Rational design of metalloenzymes: From single to multiple active sites

Artificial Metalloenzymes: Reaction Scope and Optimization Strategies

α,β‐Unsaturated 2‐Acyl‐Imidazoles in Asymmetric Biohybrid Catalysis

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