35 publications

35 publications

8-Amino-5,6,7,8-tetrahydroquinoline in Iridium(III) Biotinylated Cp* Complex as Artificial Imine Reductase

Rimoldi, I.

New J. Chem., 2018, 10.1039/C8NJ04558E

Diamine ligands I–IV coordinated to an iridium metal complex with the biotin moiety anchored to the Cp* ring were investigated. This strategy, in contrast to the traditional biotin–streptavidin technology that uses a biotinylated ligand in the artificial imine reductase, is practical for envisaging how the enantiodiscrimination by different Streptavidin (Sav) mutants could influence the chiral environment of the metal cofactor. Only in the case of (R)-CAMPY IV did the chirality at the metal centre and the second coordination sphere environment, which was dictated by the host protein, operate in a synergistic way, producing better enantioselectivity at a S112M Sav catalyst/catalyst ratio of 1.0 : 2.5. Under these optimized conditions, the artificial imine reductase afforded a good enantiomeric excess (83%) in the asymmetric transfer hydrogenation of 6,7-dimethoxy-1-methyl-3,4-dihydroisoquinoline.


Metal: Ir
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 32
ee: 83
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 99
ee: 13
PDB: ---
Notes: ---

A Dual Anchoring Strategy for the Localization and Activation of Artificial Metalloenzymes Based on the Biotin−Streptavidin Technology

Ward, T. R.

J. Am. Chem. Soc., 2013, 10.1021/ja309974s

Artificial metalloenzymes result from anchoring an active catalyst within a protein environment. Toward this goal, various localization strategies have been pursued: covalent, supramolecular, or dative anchoring. Herein we show that introduction of a suitably positioned histidine residue contributes to firmly anchor, via a dative bond, a biotinylated rhodium piano stool complex within streptavidin. The in silico design of the artificial metalloenzyme was confirmed by X-ray crystallography. The resulting artificial metalloenzyme displays significantly improved catalytic performance, both in terms of activity and selectivity in the transfer hydrogenation of imines. Depending on the position of the histidine residue, both enantiomers of the salsolidine product can be obtained.


Metal: Ir
Ligand type: Amino acid; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 14
ee: 11
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Amino acid; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 100
ee: 79
PDB: ---
Notes: ---

An Artificial Imine Reductase Based on the Ribonuclease S Scaffold

Ward, T. R.

ChemCatChem, 2014, 10.1002/cctc.201300995


Metal: Ir
Ligand type: Amino acid; Cp*
Host protein: Ribonuclease S
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 4
ee: 18
PDB: ---
Notes: ---

An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades

Ward, T. R.

J. Am. Chem. Soc., 2016, 10.1021/jacs.6b02470


Metal: Ir
Ligand type: Cp*; Phenanthroline
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: >999
ee: >99
PDB: ---
Notes: ---

Artificial Metalloenzymes Based on Biotin-Avidin Technology for the Enantioselective Reduction of Ketones by Transfer Hydrogenation

Ward, T. R.

Proc. Natl. Acad. Sci. U. S. A., 2005, 10.1073/pnas.0409684102


Metal: Ru
Ligand type: Amino-sulfonamide; P-cymene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 92
ee: 94
PDB: ---
Notes: ---

Metal: Ru
Ligand type: Amino-sulfonamide; Benzene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 30
ee: 63
PDB: ---
Notes: ---

Artificial Metalloenzymes for the Diastereoselective Reduction of NAD+ to NAD2H

Ward, T. R.

Org. Biomol. Chem., 2015, 10.1039/c4ob02071e


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: ---
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Artificial Transfer Hydrogenases Based on the Biotin-(Strept)avidin Technology: Fine Tuning the Selectivity by Saturation Mutagenesis of the Host Protein

Ward, T. R.

J. Am. Chem. Soc., 2006, 10.1021/ja061580o


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 96
ee: 80
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 73
ee: 60
PDB: ---
Notes: ---

Metal: Ru
Ligand type: Amino-sulfonamide; Benzene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 95
ee: 70
PDB: ---
Notes: ---

Metal: Ru
Ligand type: Amino-sulfonamide; P-cymene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 79
ee: 97
PDB: ---
Notes: ---

Artificial Transfer Hydrogenases for the Enantioselective Reduction of Cyclic Imines

Ward, T. R.

Angew. Chem., Int. Ed., 2011, 10.1002/anie.201007820


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 4000
ee: 96
PDB: 3PK2
Notes: ---

Metal: Rh
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 94
ee: 52
PDB: 3PK2
Notes: ---

Metal: Ru
Ligand type: Amino-sulfonamide; P-cymene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 97
ee: 22
PDB: 3PK2
Notes: ---

Metal: Ru
Ligand type: Amino-sulfonamide; Benzene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 76
ee: 12
PDB: 3PK2
Notes: ---

Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes

Ward, T. R.; Woolfson, D. N.

ACS Catal., 2018, 10.1021/acscatal.7b03773


Metal: Ir
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 970
ee: 13
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 158
ee: 82
PDB: ---
Notes: ---

Metal: Ru
Ligand type: Carbene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Reaction: Olefin metathesis
Max TON: 105
ee: ---
PDB: ---
Notes: RCM, biotinylated Hoveyda-Grubbs second generation catalyst

Metal: ---
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Reaction: Anion-π catalysis
Max TON: 6
ee: 41
PDB: ---
Notes: No metal

Computational Insights on an Artificial Imine Reductase Based on the Biotin-Streptavidin Technology

Maréchal, J.-D.

ACS Catal., 2014, 10.1021/cs400921n


Metal: Ir
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: ---
ee: 96
PDB: 3PK2
Notes: Prediction of the enantioselectivity by computational methods.

Cross-Regulation of an Artificial Metalloenzyme

Ward, T. R.

Angew. Chem., Int. Ed., 2017, 10.1002/anie.201702181


Metal: Ir
Ligand type: Cp*; Phenanthroline
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 96
ee: ---
PDB: ---
Notes: Cross-regulated reduction of the antibiotic enrofloxacin by an ArM.

Directed Evolution of an Artificial Imine Reductase

Maréchal, J.-D.; Ward, T. R.

Angew. Chem., Int. Ed., 2018, 10.1002/anie.201711016


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 380
ee: 95
PDB: 6ESS
Notes: Salsolidine formation; Sav mutant S112A-N118P-K121A-S122M: (R)-selective

Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 220
ee: 85
PDB: 6ESU
Notes: Salsolidine formation; Sav mutant S112R-N118P-K121A-S122M-L124Y: (S)-selective

Efficient in Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme

Ward, T. R.

ACS Catal., 2016, 10.1021/acscatal.6b00258


Metal: Ir
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: >1980
ee: ---
PDB: ---
Notes: ArM works in combination with the ene reductase (ER) of the Old Yellow Enzyme family fromThermus scotuductus (TsOYE).

Evaluation of Chemical Diversity of Biotinylated Chiral 1,3-Diamines as a Catalytic Moiety in Artificial Imine Reductase

Rimoldi, I.

ChemCatChem, 2016, 10.1002/cctc.201600116


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: >99
ee: 83
PDB: 3PK2
Notes: ---

Expanding the Chemical Diversity in Artificial Imine Reductases Based on the Biotin–Streptavidin Technology

Ward, T. R.

ChemCatChem, 2014, 10.1002/cctc.201300825


Metal: Ir
Ligand type: Amino acid; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 188
ee: 43
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Amino carboxylic acid; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 4
ee: 21
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 0
ee: ---
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 0
ee: ---
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Cp*; Pyrazine amide
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 26
ee: 16
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Bipyridine; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 0
ee: ---
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 12
ee: 13
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Cp*; Oxazoline
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 102
ee: 14
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Amino acid; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 94
ee: 67
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Amino amide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 10
ee: 7
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Amino carboxylic acid; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 8
ee: 1
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 6
ee: 1
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 6
ee: 1
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Cp*; Pyrazine amide
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 6
ee: 1
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Bipyridine; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 4
ee: 6
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 6
ee: 1
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Cp*; Oxazoline
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 8
ee: 0
PDB: ---
Notes: ---

Ferritin Encapsulation of Artificial Metalloenzymes: Engineering a Tertiary Coordination Sphere for an Artificial Transfer Hydrogenase

Ward, T. R.

Dalton Trans., 2018, 10.1039/C8DT02224K


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 3874
ee: 75
PDB: ---
Notes: ---

Fluorescence-Based Assay for the Optimization of the Activity of Artificial Transfer Hydrogenase within a Biocompatible Compartment

Ward, T. R.

ChemCatChem, 2013, 10.1002/cctc.201200834


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coli’s Periplasm

Ward, T. R.

J. Am. Chem. Soc., 2018, 10.1021/jacs.8b07189


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 1000
ee: 76
PDB: 6GMI
Notes: ---

Genetic Optimization of the Catalytic Efficiency of Artificial Imine Reductases Based on Biotin−Streptavidin Technology

Ward, T. R.

ACS Catal., 2013, 10.1021/cs400428r


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: ---
ee: 60
PDB: ---
Notes: ---

High-Level Secretion of Recombinant Full-Length Streptavidin in Pichia Pastoris and its Application to Enantioselective Catalysis

Jaussi, R.

Protein Expression Purif., 2014, 10.1016/j.pep.2013.10.015


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 152
ee: 61
PDB: ---
Notes: Sav expression in E. coli

Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 158
ee: 64
PDB: ---
Notes: Sav expression in P. pastoris

Human Carbonic Anhydrase II as Host Protein for the Creation of Artificial Metalloenzymes: The Asymmetric Transfer Hydrogenation of Imines

Ward, T. R.

Chem. Sci., 2013, 10.1039/c3sc51065d


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 47
ee: 70
PDB: ---
Notes: ---

Immobilization of an Artificial Imine Reductase Within Silica Nanoparticles Improves its Performance

Shahgaldian, P.; Ward, T. R.

Chem. Commun., 2016, 10.1039/c6cc04604e


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 4554
ee: 89
PDB: ---
Notes: Reaction in nanoparticles

Improving the Catalytic Performance of an Artificial Metalloenzyme by Computational Design

Baker, D.; Ward, T. R.

J. Am. Chem. Soc., 2015, 10.1021/jacs.5b06622


Metal: Ir
Ligand type: Cp*; Pyridine sulfonamide
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 100
ee: 96
PDB: ---
Notes: ---

Improving the Enantioselectivity of Artificial Transfer Hydrogenases Based on the Biotin–Streptavidin Technology by Combinations of Point Mutations

Ward, T. R.

Inorg. Chim. Acta, 2010, 10.1016/j.ica.2009.02.001


Metal: Ru
Ligand type: Amino-sulfonamide; P-cymene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 98
ee: 98
PDB: ---
Notes: ---

Metal: Ru
Ligand type: Amino-sulfonamide; Benzene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 24
ee: 84
PDB: 2QCB
Notes: ---

Library Design and Screening Protocol for Artificial Metalloenzymes Based on the Biotin-Streptavidin Technology

Ward, T. R.

Nat. Protoc., 2016, 10.1038/nprot.2016.019


Metal: Ir
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 183
ee: 71
PDB: ---
Notes: Purified streptavidin (mutant K121A)

Metal: Ir
Ligand type: Cp*; Diamine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 42
ee: 59
PDB: ---
Notes: Cell free extract (mutant Sav K121A) treated with diamide

Metal: Ru
Ligand type: N-heterocyclic carbene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 66
ee: ---
PDB: ---
Notes: Purified streptavidin (mutant K121A)

Metal: Ru
Ligand type: N-heterocyclic carbene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 18
ee: ---
PDB: ---
Notes: Cell free extract (mutant Sav K121A immobilised on iminobiotin-sepharose beads)

Neutralizing the Detrimental Effect of Glutathione on Precious Metal Catalysts

Ward, T. R.

J. Am. Chem. Soc., 2014, 10.1021/ja500613n


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 98
ee: 85
PDB: ---
Notes: Reaction in cell-free extract with diamide

Piano-Stool d(6)-Rhodium(III) Complexes of Chelating Pyridine-Based Ligands and their Papain Bioconjugates for the Catalysis of Transfer Hydrogenation of Aryl Ketones in Aqueous Medium

Mangiatordi, G. F.; Salmain, M.

J. Mol. Catal. B: Enzym., 2015, 10.1016/j.molcatb.2015.10.007


Metal: Rh
Ligand type: Cp*; Phenanthroline
Host protein: Papain (PAP)
Anchoring strategy: Covalent
Optimization: Chemical
Max TON: 30
ee: 9
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Cp*; Di(2-pyridyl)
Host protein: Papain (PAP)
Anchoring strategy: Covalent
Optimization: Chemical
Max TON: 20
ee: 5
PDB: ---
Notes: ---

Porous Protein Crystals as Catalytic Vessels for Organometallic Complexes

Kitagawa, S.; Ueno, T.

Chem. - Asian J., 2014, 10.1002/asia.201301347


Metal: Ru
Ligand type: Benzene
Host protein: Lysozyme (crystal)
Anchoring strategy: Dative
Optimization: ---
Max TON: ---
ee: ---
PDB: 3W6A
Notes: Tetragonal HEWL crystals

Metal: Ru
Ligand type: Benzene
Host protein: Lysozyme (crystal)
Anchoring strategy: Dative
Optimization: ---
Max TON: ---
ee: ---
PDB: 4J7V
Notes: Orthorhombic HEWL crystals

Proteins as Macromolecular Ligands for Metal-Catalysed Asymmetric Transfer Hydrogenation of Ketones in Aqueous Medium

Salmain, M.

Eur. J. Inorg. Chem., 2018, 10.1002/ejic.201701359


Metal: Ru
Ligand type: Benzene derivatives
Anchoring strategy: Undefined
Optimization: ---
Max TON: 43
ee: 82
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Cp*
Anchoring strategy: Undefined
Optimization: ---
Max TON: 16
ee: 14
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Cp*
Anchoring strategy: Undefined
Optimization: ---
Max TON: 20
ee: 16
PDB: ---
Notes: ---

Redox-Switchable Siderophore Anchor Enables Reversible Artificial Metalloenzyme Assembly

Duhme-Klair, A. K.; Wilson, K. S.

Nat. Catal., 2018, 10.1038/s41929-018-0124-3


Metal: Ir
Ligand type: Cp*; Pyridine sulfonamide
Host protein: CeuE
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: ---
ee: 35.4
PDB: 5OD5
Notes: Redox switchable iron(III)-azotochelin anchor