Tailoring the Active Site of Chemzymes by Using a Chemogenetic‐Optimization Procedure: Towards Substrate‐Specific Artificial Hydrogenases Based on the Biotin–Avidin Technology

Klein, Gérard; Humbert, Nicolas; Gradinaru, Julieta; Ivanova, Anita; Gilardoni, François; Rusbandi, Untung E.; Ward, Thomas R.

doi:10.1002/anie.200502000

Cited by 110 publications

(64 citation statements)

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“…This chemo-genetic optimization scheme (a term initially coined by Distefano [13] ) allows the rapid generation of substrate-specific and either (R)-or (S)-selective artificial metalloenzymes (Table 1). [26] These results highlight the versatility of the chemogenetic optimization scheme. The natures of the spacer, the ligand, and the aminoacid residue at position 112, identified as a close-lying residue (Table 1, entry 2), all work in concert to afford either (R)-or (S)-selective catalysts (up to 94 % ee (R), Table 1, entries 1, 3 and 9; up to 88 % ee (S), Table 1, entries 4-7).…”

Section: Supramolecular Anchoring Strategiesmentioning

confidence: 82%

Artificial Metalloenzymes for Enantioselective Catalysis: Recent Advances

Letondor

Ward

2007

ChemInform

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Section: Supramolecular Anchoring Strategiesmentioning

confidence: 82%

Artificial Metalloenzymes for Enantioselective Catalysis: Recent Advances

Letondor

Ward

2007

ChemInform

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“…[21][22][23][24] βGAL was chosen as donor mainly because of its strong fluorescence emission from abundant Trp residues at UV excitation. It is an enzyme containing 156 Trp residues and is widely distributed in microorganisms, animals and plants.…”

Section: 20mentioning

confidence: 99%

Multidonor Deep-UV FRET Study of Protein–Ligand Binding and Its Potential to Obtain Structure Information

Seeger

2011

J. Phys. Chem. B

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Fluorescence resonance energy transfer (FRET) using biotinylated -galactosidase (GAL) as donor and Alexa Fluor 350 (AF350) labelled avidin as acceptor has been investigated by means of steady-state fluorescence and time-resolved fluorescence spectroscopy. The donors are readily paired with acceptors through the well-established binding affinity of biotin and avidin. The fluorescence energy transfer efficiency was determined by the donor fluorescence emission and lifetime changes in the presence and absence of acceptor. The theoretical energy transfer efficiency and theoretical average distance between donor and acceptor after non-covalent binding was calculated by taking the distribution of tryptophan residues in GAL and avidin as well as the location of AF350 in avidin into account, which agree with the experimental data. It is shown how information of the location of acceptor can be obtained. Further, the fluorescence intensity image of AF350 on biotinylated GAL coated quartz surface through UV FRET has been recorded using deep UV laser-based fluorescence lifetime microscopy. The results demonstrate that (a) deep UV laser-based fluorescence lifetime microscopy is a simple and useful method to study UV FRET of proteins using intrinsic fluorescence, (b) structural information even in complex multi-donor systems can be obtained and (c) FRET signals can be obtained to detect binding events using the native fluorescence of proteins as multi-donor systems.

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“…[10] In most cases, the chemical optimization such as using a conformationally rigid biotin spacer containing enantiopure amino acids [9,11] has a larger impact on the performance of the hybrid catalyst than exchange of an amino acid of the protein.…”

Section: Artificial Metalloenzymes: Enantioselective Catalysis and Bementioning

confidence: 99%

Bioorganic and Bioinorganic Chemistry

Constable¹,

Housecroft²,

Creus³

et al. 2010

Chimia

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The interdisciplinary projects in bioinorganic and bioorganic chemistry of the Department of Chemistry, University of Basel led to the preparation of new systems that mimic biologically important processes and to the discovery of compounds from natural sources which are very promising with respect to medical applications. The advances in these areas are reported here. The Constable-Housecroft group is involved in biomimetic and bioinspired chemistry primarily relating to the fundamental processes in nature with a target of designing functional systems of sufficient robustness for practical application. This overview concentrates upon chemical approaches to the splitting of water into H 2 and O 2 based upon biomimetic or bioinspired principles. Other activities within the group involve the tagging of biomolecules with luminescent metal complexes for intracellular studies (with Prof. Matthias Wymann, Department of Biomedicine) and the deployment of nanoparticles functionalised with laccase for water purification (with Prof. Uwe Pieles, FHNW). The group has adopted a general strategy of mimicking the biological membrane by using two-dimensional control of the self-assembly of multiple components at solid-liquid or solid-air interfaces.The ultimate aim for energy production is a coupled water-splitting reaction using solar energy to generate H 2 and O 2 followed by recombination of the two diatomics in a fuel cell. The formal process is presented in Fig. 1 which serves to highlight the features that need to be controlled. Water oxidation and reduction reactions will take place at spatially separated sites and the kinetics of charge separation will be critical in controlling the success of the devices. The device can be purely molecular or the oxidation and reduction equivalents could be holes and electrons in the valence and conduction bands of a semiconductor or a combination of both approaches.For the water reduction process the group has taken inspiration from the Fe 2 S 2 structural motif found in Fe-Fe hydrogenases and invested significant synthetic Biomimetic Splitting of WaterEdwin C. Constable and Catherine E. Housecroft Evolutionary Rules for Metalloenzyme Design Marc CreusCurrent work within the newlyestablished Creus group is based on the concept that direct metal coordination to non-catalytic proteins may lead to nascent metalloenzymes, which can form a basis for further evolution. Conceptually, the dual ideas of 'emergence' and 'evolution' of metalloenzymes correspond to two extremes of an evolutionary process: i) a qualitative step, involving a new function reached through innovation (e.g. acquisition of catalytic activity from previously inactive form) and ii) a quantitative step (e.g. the improvement of a weak, but detectable function). Directed evolution, despite its limitations in practical terms, [1] provides a powerful tool for the second type (or quantitative) step. [2] Although the study of intermediate steps of improvement of metalloenzymes is likely to contribute greatly to the ...

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Tailoring the Active Site of Chemzymes by Using a Chemogenetic‐Optimization Procedure: Towards Substrate‐Specific Artificial Hydrogenases Based on the Biotin–Avidin Technology

Cited by 110 publications

References 50 publications

Artificial Metalloenzymes for Enantioselective Catalysis: Recent Advances

Artificial Metalloenzymes for Enantioselective Catalysis: Recent Advances

Multidonor Deep-UV FRET Study of Protein–Ligand Binding and Its Potential to Obtain Structure Information

Bioorganic and Bioinorganic Chemistry

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