Artificial Metalloenzymes Publications @Ward Group
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  • Ligand type
    • 1,2-diaminocyclohexane
    • 2,2-[(1,2-ethanediyl)bis(nitrilopropylidyne)]bisphenol
    • 2,2'-Dipyridylamine
    • [4Fe-4S] cofactor
    • 9-mesityl-10-phenyl acridinium
    • Acac
    • Allyl
    • Amine
    • Amino acid
    • Amino amide
    • Amino carboxylic acid
    • Amino-sulfonamide
    • Arene
    • Azadithiolate (SCH2NHCH2S)
    • Benzene
    • Benzene derivatives
    • Bidentate ligands
    • biotinylated [Fe–Fe] hydrogenase organometallic mimic
    • Biotinylated naphthalenediimid
    • Biotinylated pyrrolidine
    • Bipyridine
    • Bis(2-(pyridin-2-yl)ethyl)amine
    • Bisdiphosphine
    • Bisimidazol
    • BPHMEN
    • BPMCN
    • BPMEN
    • Bypyridine
    • C6Me6
    • Carbene
    • Carbonyl
    • Carboxylate
    • CN
    • CO
    • CO2
    • COD
    • Copper cluster
    • Corrole
    • Cp
    • Cp*
    • C-T mismatch
    • Cu(dmbipy)(NO3)2
    • Cyclooctadiene
    • Cyclopentadienone
    • Cyclopentadienyl
    • Deuteroporphyrin IX
    • Di(2-pyridyl)
    • Diamine
    • Diphenylphosphine
    • Dipyridin-2-ylmethane
    • Dirhodium
    • Diselenolate
    • Dithiolate
    • DNA (G quadruplex)
    • Double winged protoporphyrin IX
    • EDTA
    • Flavin
    • Histidine residues
    • Hoveyda–Grubbs
    • Hydroxaamate
    • Hydroxyquinoline
    • Maleimide-protoporphyrin IX
    • Methyl
    • N'-(2-hydroxybenzyl)-N,N'-ethylenediamine
    • NCN-Pincer (amines)
    • N-heterocyclic carbene
    • N-methyl histidine
    • N,N,N’,N’-tetraethyldiethylene triamine (TEDETA)
    • Norbornadiene
    • Nδ-methylhistidine
    • OAc
    • OH
    • OMe
    • Oxazoline
    • Oxide
    • Oxime
    • P-cymene
    • Phenanthroline
    • Phenolate
    • Phosphine
    • Phthalocyanine
    • Poly-carboxylic acid
    • Poly-pyridine
    • Porphycene
    • Porphyrin
    • Protoporphyrin IX
    • Pyrazine amide
    • Pyrazole
    • Pyridine
    • Pyridine sulfonamide
    • Pyridone
    • Quinoline
    • RNA
    • Salen
    • Salophen
    • Single winged protoporphyrin IX
    • Terpyridine
    • Tetra-aryl-substituted porphyrin
    • Tetradehydrocorrin
    • Tetramine
    • Tetraphenyl cyclopentadiene
    • Tetrathiolate
    • Thioether (Pincer complex)
    • Tripeptide
    • Tris(pyridylmethyl)amine (TPA)
    • Undefined
    • Water
  • Host protein
    • 6-Phospho-gluconolactonase (6-PGLac)
    • A2A adenosine receptor
    • Adipocyte lipid binding protein (ALBP)
    • Alcohol dehydrogenase
    • Antibody
    • Antibody 03-1
    • Antibody 12E11G
    • Antibody 13G10
    • Antibody 13G10 / 14H7
    • Antibody 14H7
    • Antibody 1G8
    • Antibody 28F11
    • Antibody 38C2
    • Antibody 3A3
    • Antibody 7A3
    • Antibody7G12-A10-G1-A12
    • Antibody L-chain from Mab13-1 hybridoma cells
    • Antibody SN37.4
    • Apo-[Fe]-hydrogenase from M. jannaschii
    • Apo-ferritin
    • Apo-HydA1 ([FeFe]-hydrogenase) from C. reinhardtii
    • Apo-HydA enzymes from C. reinhardtii, M. elsdenii, C. pasteurianum
    • Artificial bidomain repeat protein, (A3A3′)Y26C
    • Artificial construct
    • Aspertate dehydrogenase
    • Avidin (Av)
    • Azurin
    • Binding domain of Rabenosyn (Rab4)
    • Bovine carbonic anhydrase (CA)
    • Bovine carbonic anhydrase II (CA)
    • Bovine serum albumin (BSA)
    • Bovine β-lactoglobulin (βLG)
    • Bromelain
    • Burkavidin
    • C45 (c-type cytochrome maquette)
    • Carbonic anhydrase (CA)
    • Carboxypeptidase A
    • Catabolite activator protein (CAP)
    • CeuE
    • CO2-reducing photosensitizer protein (PSP)
    • C-terminal domain of calmodulin
    • Cupin superfamily protein (TM1459)
    • Cupredoxin
    • Cutinase
    • CYP119
    • Cytochrome b562
    • Cytochrome BM3h
    • Cytochrome c
    • Cytochrome c552
    • Cytochrome cb562
    • Cytochrome c peroxidase
    • Cytochrome P450 (CYP119)
    • DADA dipeptide
    • De novo-designed protein
    • DNA
    • Domain of Hin recombinase
    • Due Ferri
    • E. coli catabolite gene activator protein (CAP)
    • [FeFe]-hydrogenase from C. pasteurianum (CpI)
    • Ferredoxin (Fd)
    • Ferric hydroxamate uptake protein component: A (FhuA)
    • Ferric hydroxamate uptake protein component: A (FhuA) ΔCVFtev
    • Ferritin
    • Flavodoxin (Fld)
    • Folypolyglutamate synthase
    • GCN4 bZIP transcription factor (brHis2)
    • Glyoxalase II (Human)
    • (gp27-gp5)3
    • gp45
    • [(gp5βf)3]2
    • HasA
    • Heme oxygenase (HO)
    • Hemoglobin
    • Horse heart cytochrome c
    • Horseradish peroxidase (HRP)
    • Human carbonic anhydrase
    • Human carbonic anhydrase II (hCAII)
    • Human retinoid-X-receptor (hRXRa)
    • Human serum albumin (HSA)
    • HydA1 ([FeFe]-hydrogenase) from C. reinhardtii
    • IgG 84A3
    • Laccase
    • Lactoccal multidrug resistant regulator (LmrR)
    • Lipase B from C. antarctica (CALB)
    • Lipase from G. thermocatenulatus (GTL)
    • Lysozyme
    • Lysozyme (crystal)
    • Maltose-binding protein (MBP)
    • Manganese Porphyrin-binding Protein 1
    • metalloDNAzyme
    • Metallo-β-lactamase (AB5)
    • Mimochrome Fe(III)-S6G(D)-MC6 (De novo designed peptide)
    • Monomeric Teal FP (mTFP)
    • Mouse adenosine deaminase
    • Myoglobin (Mb)
    • Neocarzinostatin (variant 3.24)
    • NikA
    • Nitrobindin (Nb)
    • Nitrobindin variant NB4
    • Nuclease from S. aureus
    • Papain (PAP)
    • Phosphoribosylamine - glycine ligase
    • Photoactive Yellow Protein (PYP)
    • Photosystem I (PSI)
    • Phytase
    • Prolyl oligopeptidase (POP)
    • Prolyl oligopeptidase (POP) from P. furiosus
    • Pseudomonas savastanoi ethylene-forming enzyme (PsEFE)
    • R2-like ligand-binding oxidase (R2lox)
    • Rabbit serum albumin (RSA)
    • Ribonuclease S
    • RNA
    • RNase A
    • Rubredoxin (Rd)
    • Silk fibroin fibre
    • Small heat shock protein from M. jannaschii
    • ß-lactoglobulin
    • Staphylococcal nuclease
    • Steroid Carrier Protein 2L (SCP-2L)
    • Sterol Carrier Protein (SCP)
    • Streptavidin (monmeric)
    • Streptavidin (Sav)
    • Superoxide dismutase (SOD)
    • Synthetic peptide
    • Thermolysin
    • Thermosome (THS)
    • tHisF
    • TM1459 cupin
    • TRI peptide
    • Trypsin
    • Tryptophan gene repressor (trp)
    • Ubiquitin
    • Uno Ferro single chain (4G-UFsc)
    • Xylanase A (XynA)
    • Zn8:AB54
    • Zn8:AB54 (mutant C96T)
    • α3D peptide
    • α-chymotrypsin
    • β-lactamase
    • β-lactoglobulin (βLG)
  • Anchoring
    • Amino acid
    • Antibody
    • Antigen
    • Covalent
    • Cystein-maleimide
    • Dative
    • Heme
    • Hydrogen bond
    • Imidazole ligandoside
    • Lysine-succinimide
    • Metal substitution
    • Native
    • Non-natural aminoacid
    • Reconstitution
    • Supramolecular
    • Undefined
  • Optimization
    • Chemical
    • Chemical & computational design
    • Chemical & genetic
    • Computational design
    • Genetic
  • Reaction
    • 4-amino-phenol oxidation
    • Acylation
    • Alcohol oxidation
    • Aldol condensation
    • Alkene–alkyne coupling
    • Allylic alkylation
    • Allylic amination
    • Amine oxidation
    • Anion-π catalysis
    • Baylis-Hillman reaction
    • B-H insertion
    • Carbene insertion
    • Catechol oxidation
    • CCO oxidase activity
    • C-H activation
    • C-H amination
    • C-H functionalization
    • C-H insertion
    • C-H oxidation
    • CO2 reduction
    • Cross-coupling
    • Cycloaddition
    • Cyclopropanation
    • Deallylation
    • Depropargylation
    • Diazo cross-coupling
    • Diels-Alder cycloaddition
    • Diels-Alder reaction
    • Dihydroxylation
    • DNA cleavage
    • Electron/Proton transfer
    • Electron transfer
    • Epoxidation
    • Epoxide ring opening reaction
    • Ester hydrolysis
    • Fridel-Crafts reaction
    • Friedel-Crafts alkylation
    • H2 evolution
    • H2 evolution / H2 oxidation
    • Heck cross-coupling
    • Hydration
    • Hydration of C=C and C=O double bonds
    • Hydroamination
    • Hydroformylation
    • Hydrogenation
    • Hydrogenation / H2 evolution
    • Hydrolysis
    • Hydrolytic cleavage
    • Hydroxychlorination
    • Hydroxylation
    • Inverse electron-demand hetero-Diels–Alder (IEDHDA)
    • Kemp elimination
    • Lactam synthesis
    • Lignin oxidation
    • Metal substitution
    • Methane generation
    • Michael addition
    • N-H Insertion
    • N-Hydroxylation
    • Nicotinamide reduction
    • NO reduction
    • O2 reduction
    • Olefin metathesis
    • Oxidation
    • Oxidation of aryl sulphides
    • Oxidation of hydroxylamines
    • Oxidation of styrenes
    • Oxidative cleavage
    • Peroxidase activity
    • Peroxidation
    • Peroxidation or oxygenation
    • Phenylacetylene polymerization
    • Photooxidation
    • Polymerization
    • Protein and nucleic acid oxidative cleavage
    • Reduction
    • Reductive debromination
    • Ring closing metathesis
    • RNA ligation
    • S-H insertion
    • Si-H insertion
    • Small-molecule reduction
    • Sulfite reduction
    • Sulfoxidation
    • Suzuki coupling
    • Suzuki cross-coupling
    • Suzuki-Miyaura coupling
    • Transamination
    • Transfer hydrogenation
    • Water addition
    • Water oxidation
  • Corresponding author
    • Akabori, S.
    • Alberto, R.
    • Albrecht, M.
    • Anderson, J.L.R.
    • Apfel, U.-P.
    • Arada, H.
    • Arnold, F.H.
    • Arold, S.T.
    • Arseniyadis, S.
    • Artero, V.
    • Bäckvall, J.E.
    • Baker, D.
    • Ball, Z.T.
    • Banse, F.
    • Barker, P.D.
    • Berggren, G.
    • Bian, H.-D.
    • Birnbaum, E.R.
    • Borovik, A.S.
    • Boss, S.R.
    • Bren, K.L.
    • Bruns, N.
    • Brustad, E.M.
    • Campagne, J.
    • Cardona, F.
    • Case, M.A.
    • Cavazza, C.
    • Chakraborty, S.
    • Chan, A.S.C.
    • Chen, Y.
    • Clark, D.S.
    • Clever, G.H.
    • Coleman, J.E.
    • Craik, C.S.
    • Creus, M.
    • Cuatrecasas, P.
    • Darnall, D.W.
    • DeGrado, W.F.
    • Dervan, P.B.
    • de Vries, J.
    • Diéguez, M.
    • Distefano, M.D.
    • Dömötör, O.
    • Don Tilley, T.
    • Duhme-Klair, A.K.
    • Ebright, R.H.
    • Emerson, J.P.
    • Enyedy, É.A.
    • Eppinger, J.
    • Fasan, R.
    • Filice, M.
    • Fontecave, M.
    • Fontecilla-Camps, J.C.
    • Fruk, L.
    • Fujieda, N.
    • Fussenegger, M.
    • Gademann, K.
    • Gaggero, N.
    • Gao, X.
    • Garribba, E.
    • Germanas, J.P.
    • Ghattas, W.
    • Ghirlanda, G.
    • Golinelli-Pimpaneau, B.
    • Goti, A.
    • Gras, E.
    • Gray, H.B.
    • Green, A.P.
    • Groll, M.
    • Gross, Z.
    • Gunasekeram, A.
    • Happe, T.
    • Harada, A.
    • Hartwig, J.F.
    • Hasegawa, J.-Y.
    • Hayashi, T
    • Head-Gordon, T.
    • Hemschemeier, A.
    • Hendrich, M.P.
    • Herrick, R.S.
    • Hilvert, D.
    • Hirota, S.
    • Höcker, B.
    • Holland, P.L.
    • Hromadová, M.
    • Huang, F.-P.
    • Hureau, C.
    • Hu, X.
    • Hyster, T.K.
    • Imanaka, T.
    • Imperiali, B.
    • Itoh, S.
    • Jäger, C.M.
    • Janda, K.D.
    • Jarvis, A.G.
    • Jaussi, R.
    • Jeschek, M.
    • Jiménez-Osés, G.
    • Kaiser, E.T.
    • Kamer, P.C.J.
    • Kazlauskas, R.J.
    • Keasling, J.D.
    • Kehl-Fie, T.E.
    • Keinan, E.
    • Khare, S.D.
    • Kim, H.M.
    • Kim, H.S.
    • Kitagawa, S.
    • Klein Gebbink, R.J.M.
    • Koenigs, R.M.
    • Kokubo, T.
    • Korendovych, I.V.
    • Kuhlman, B.
    • Kurisu, G.
    • Laan, W.
    • Latour, J.-M.
    • Lechner, H.
    • Lee, H.S.
    • Lee, S.-Y.
    • Lehnert, N.
    • Leow, T.C.
    • Lerner, R.A.
    • Lewis, J.C.
    • Liang, H.
    • Li, C.
    • Lindblad, P.
    • Lin, Y.-W.
    • Liu, J.
    • Liu, P.
    • Liu, X.
    • Lombardi, A.
    • Louro, R.O.
    • Lubitz, W.
    • Luk, L.Y.P.
    • Lu, Y.
    • Maglio, O.
    • Mahy, J.-P.
    • Makhlynets, O.V.
    • Mangiatordi, G.F.
    • Marchetti, M.
    • Marchi-Delapierre, C.
    • Maréchal, J.-D.
    • Marino, T.
    • Marshall, N.M.
    • Mascareñas, J.L.
    • Matile, S.
    • Matsuo, T.
    • Mayer, C.
    • McNaughton, B.R.
    • Ménage, S.
    • Messori, L.
    • Moënne-Loccoz, P.
    • Mukhopadhyay, A.
    • Mulfort, K.L.
    • Nastri, F.
    • Nelson, H.M.
    • Nicewicz, D.A.
    • Nicholas, K.M.
    • Niemeyer, C.M.
    • Nolte, R.J.M.
    • Novič, M.
    • Okamoto, Y.
    • Okano, M.
    • Okuda, J.
    • Onoda, A.
    • Oohora, K.
    • Palomo, J.M.
    • Pàmies, O.
    • Panke, S.
    • Pan, Y.
    • Paradisi, F.
    • Peacock, A.F.A.
    • Pecoraro, V.L.
    • Pellegrino, S.
    • Pordea, A.
    • Reetz, M.T.
    • Reijerse, E.
    • Renaud, J.-L.
    • Ricoux, R.
    • Rimoldi, I.
    • Roelfes, G.
    • Roux, B.
    • Rovis, T.
    • Sakurai, S.
    • Salmain, M.
    • Sasaki, T.
    • Sauer, D.F.
    • Schultz, P.G.
    • Schwaneberg, U.
    • Seelig, B.
    • Shafaat, H.S.
    • Shahgaldian, P.
    • Shaw, W.J.
    • Sheldon, R.A.
    • Shima, S.
    • Shoji, O.
    • Sigman, D.S.
    • Smietana, M.
    • Song, W.J.
    • Soumillion, P.
    • Strater, N.
    • Sugiura, Y.
    • Szostak, J.W.
    • Tanaka, K.
    • Tezcan, F.A.
    • Thorimbert, S.
    • Tian, C.
    • Tiede, D.M.
    • Tiller, J.C.
    • Turner, N.J.
    • Ueno, T.
    • Utschig, L.M.
    • van Koten, G.
    • Waldron, K.J.
    • Wang, C.
    • Wang, J.
    • Ward, T.R.
    • Watanabe, Y.
    • Webster, A.M.
    • Weissenborn, M.J.
    • Whitesides, G.M.
    • Wilson, K.S.
    • Woolfson, D.N.
    • Wu, Y.
    • Yamaguchi, H.
    • Yilmaz, F.
    • Zeymer, C.
    • Zhang, J.-L.
    • Zhao, L.
    • Zhong, F.
  • Journal
    • 3 Biotech
    • Acc. Chem. Res.
    • ACS Catal.
    • ACS Cent. Sci.
    • ACS Sustainable Chem. Eng.
    • Adv. Synth. Catal.
    • Angew. Chem.
    • Angew. Chem. Int. Ed.
    • Appl. Biochem. Biotechnol.
    • Appl. Organomet. Chem.
    • Artificial Metalloenzymes and MetalloDNAzymes in Catalysis: From Design to Applications
    • Beilstein J. Org. Chem.
    • Biochemistry
    • Biochim. Biophys. Acta, Bioenerg.
    • Biochimie
    • Bioconjug. Chem.
    • Biomacromolecules
    • Bioorg. Med. Chem.
    • Bioorg. Med. Chem. Lett.
    • Bioorganometallic Chemistry: Applications in Drug Discovery, Biocatalysis, and Imaging
    • Biopolymers
    • Biotechnol. Adv.
    • Biotechnol. Appl. Biochem.
    • Biotechnol. Bioeng.
    • BCSJ
    • Can. J. Chem.
    • Catal. Lett.
    • Catal. Sci. Technol.
    • Cat. Sci. Technol.
    • ChemBioChem
    • ChemCatChem
    • Chem. Commun.
    • Chem. Rev.
    • Chem. Sci.
    • Chem. Soc. Rev.
    • Chem. - Eur. J.
    • Chem. Eur. J.
    • Chem. - Asian J.
    • Chem. Lett.
    • ChemistryOpen
    • ChemPlusChem
    • ChemSusChem
    • Chimia
    • Commun. Chem.
    • Comprehensive Inorganic Chemistry II
    • Comprehensive Supramolecular Chemistry II
    • C. R. Chim.
    • Coordination Chemistry in Protein Cages: Principles, Design, and Applications
    • Coord. Chem. Rev.
    • Croat. Chem. Acta
    • Curr. Opin. Biotechnol.
    • Curr. Opin. Chem. Biol.
    • Curr. Opin. Green Sustain. Chem.
    • Curr. Opin. Struct. Biol.
    • Dalton Trans.
    • Effects of Nanoconfinement on Catalysis
    • Energy Environ. Sci.
    • Eur. J. Biochem.
    • Eur. J. Inorg. Chem.
    • Faraday Discuss.
    • FEBS Lett.
    • Helv. Chim. Acta
    • Inorg. Chim. Acta
    • Inorg. Chem.
    • Int. J. Mol. Sci.
    • Isr. J. Chem.
    • Johnson Matthey Technol. Rev.
    • J. Biol. Chem.
    • J. Biol. Inorg. Chem.
    • J. Electroanal. Chem.
    • J. Immunol. Methods
    • J. Inorg. Biochem.
    • J. Mol. Catal. A: Chem.
    • J. Mol. Catal. B: Enzym.
    • J. Organomet. Chem.
    • J. Phys. Chem. Lett.
    • J. Porphyr. Phthalocyanines
    • J. Protein Chem.
    • J. Am. Chem. Soc.
    • J. Chem. Soc.
    • J. Chem. Soc., Chem. Commun.
    • Methods Enzymol.
    • Mol. Divers.
    • Molecular Encapsulation: Organic Reactions in Constrained Systems
    • Nature
    • Nat. Catal.
    • Nat. Chem. Biol.
    • Nat. Chem.
    • Nat. Commun.
    • Nat. Protoc.
    • Nat. Rev. Chem.
    • New J. Chem.
    • Org. Biomol. Chem.
    • Org. Biomol. Chem.
    • Organometallics
    • PLoS One
    • Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci.
    • Proc. Natl. Acad. Sci. U.S.A.
    • Proc. Natl. Acad. Sci. U. S. A.
    • Process Biochem.
    • Prog. Inorg. Chem.
    • Prot. Eng.
    • Protein Eng. Des. Sel.
    • Protein Engineering Handbook
    • Protein Expression Purif.
    • Pure Appl. Chem.
    • RSC Adv.
    • RSC Chem. Biol.
    • Science
    • Sci. Adv.
    • Sci. Rep.
    • Small
    • Synlett
    • Synth. Syst. Biotechnol.
    • Tetrahedron
    • Tetrahedron: Asymmetry
    • Tetrahedron Lett.
    • Chem. Rec.
    • Top. Catal.
    • Top. Organomet. Chem.
    • Trends Biotechnol.
  • Type
    • Article
    • Review
  • Date
    • 2022
    • 2021
    • 2020
    • 2019
    • 2018
    • 2017
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    • 1956

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