Biotransformations

Gideon Grogan

Annu. Rep. Prog. Chem., Sect. B: Org. Chem., 2009, 105, 206
DOI: 10.1039/b822048b

Lipase active site covalent anchoring of Rh(NHC) catalysts: towards chemoselective artificial metalloenzymes

M. Basauri-Molina, C. F. Riemersma, M. A. Würdemann, H. Kleijn and R. J. M. Klein Gebbink

Chem. Commun., 2015, 51, 6792
DOI: 10.1039/C4CC09700A

Design and engineering of artificial oxygen-activating metalloenzymes

Flavia Nastri, Marco Chino, Ornella Maglio, Ambika Bhagi-Damodaran, Yi Lu and Angela Lombardi

Chem. Soc. Rev., 2016, 45, 5020
DOI: 10.1039/C5CS00923E

Neocarzinostatin-based hybrid biocatalysts for oxidation reactions

Elodie Sansiaume-Dagousset, Agathe Urvoas, Kaouthar Chelly, Wadih Ghattas, Jean-Didier Maréchal, Jean-Pierre Mahy and Rémy Ricoux

Dalton Trans., 2014, 43, 8344
DOI: 10.1039/C4DT00151F

Selective oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of hemozymes

Rémy Ricoux, Mathieu Allard, Roger Dubuc, Claude Dupont, Jean-Didier Maréchal and Jean-Pierre Mahy

Org. Biomol. Chem., 2009, 7, 3208
DOI: 10.1039/b907534h

Schiff base complex conjugates of bovine serum albumin as artificial metalloenzymes for eco-friendly enantioselective sulfoxidation

Jie Tang, Pengfei Yao, Lina Wang, Hedong Bian, Meiyi Luo and Fuping Huang

RSC Adv., 2018, 8, 40720
DOI: 10.1039/C8RA07113F

Bovine serum albumin–cobalt(ii) Schiff base complex hybrid: an efficient artificial metalloenzyme for enantioselective sulfoxidation using hydrogen peroxide

Jie Tang, Fuping Huang, Yi Wei, Hedong Bian, Wei Zhang and Hong Liang

Dalton Trans., 2016, 45, 8061
DOI: 10.1039/C5DT04507J

Effect of distal histidines on hydrogen peroxide activation by manganese reconstituted myoglobin

Yuan-Bo Cai, Xiao-Han Li, Jing Jing and Jun-Long Zhang

Metallomics, 2013, 5, 828
DOI: 10.1039/c3mt20275e

The structure and peroxidase activity of myoglobin in alcoholic solvents

Andrew Long, Paul Rothenberg, Dhea Patel, Julia MacDougall and Matthew R. Hartings

Polyhedron, 2016, 114, 138
DOI: 10.1016/j.poly.2015.11.028

Artificial Enzyme Design with Novel Functions via Site‐Specific Chemical Modification

Zhixi Zhu and Zhi Zhou

ChemBioChem, 2025, 26
DOI: 10.1002/cbic.202500075

The Important Role of Covalent Anchor Positions in Tuning Catalytic Properties of a Rationally Designed MnSalen-Containing Metalloenzyme

Dewain K. Garner, Lei Liang, David A. Barrios, Jun-Long Zhang and Yi Lu

ACS Catal., 2011, 1, 1083
DOI: 10.1021/cs200258e

A Ligand Structure–Activity Study of DNA‐Based Catalytic Asymmetric Hydration and Diels–Alder Reactions.

Fiora Rosati and Gerard Roelfes

ChemCatChem, 2011, 3, 973
DOI: 10.1002/cctc.201000440

Bioinspired Catalyst Design and Artificial Metalloenzymes

Peter J. Deuss, René den Heeten, Wouter Laan and Paul C. J. Kamer

Chemistry A European J, 2011, 17, 4680
DOI: 10.1002/chem.201003646

Directed evolution enhances the peroxidation activity of myoglobin reconstituted with an iron corrole complex

Koki Takeuchi, Shunsuke Kato, Rina Ueshima and Takashi Hayashi

Bulletin of the Chemical Society of Japan, 2026, 99
DOI: 10.1093/bulcsj/uoag024

Protein-based hybrid catalysts—design and evolution

Valentin Köhler, Yvonne M Wilson, Cheikh Lo, Alessia Sardo and Thomas R Ward

Current Opinion in Biotechnology, 2010, 21, 744
DOI: 10.1016/j.copbio.2010.09.004

Stereoselective sulfoxidation catalyzed by achiral Schiff base complexes in the presence of serum albumin in aqueous media

Jie Tang, Pengfei Yao, Fuping Huang, Meiyi Luo, Yi Wei and Hedong Bian

Tetrahedron: Asymmetry, 2017, 28, 1700
DOI: 10.1016/j.tetasy.2017.10.021

Regioselective Hydroformylation of Styrene Using Rhodium‐Substituted Carbonic Anhydrase

Qing Jing and Romas J. Kazlauskas

ChemCatChem, 2010, 2, 953
DOI: 10.1002/cctc.201000159

Reconstitution of Myoglobin with Iron Porphycene Generates an Artificial Aldoxime Dehydratase with Expanded Catalytic Activities

Shunsuke Kato, Miteki Abe, Harald Gröger and Takashi Hayashi

ACS Catal., 2024, 14, 13081
DOI: 10.1021/acscatal.4c03220

Noncovalent Modulation of pH‐Dependent Reactivity of a Mn–Salen Cofactor in Myoglobin with Hydrogen Peroxide

Jun‐Long Zhang, Dewain K. Garner, Lei Liang, David A. Barrios and Yi Lu

Chemistry A European J, 2009, 15, 7481
DOI: 10.1002/chem.200802449

Various strategies for obtaining oxidative artificial hemoproteins with a catalytic oxidative activity: from "Hemoabzymes" to "Hemozymes"?

Jean-Pierre Mahy, Jean-Didier Maréchal and Rémy Ricoux

J. Porphyrins Phthalocyanines, 2014, 18, 1063
DOI: 10.1142/S1088424614500813

Supramolecular Anchoring of NCN‐Pincer Palladium Complexes into a β‐Barrel Protein Host: Molecular‐Docking and Reactivity Insights

Lucrèce Pocquet, Nikolay Vologdin, Giuseppe Felice Mangiatordi, Ilaria Ciofini, Orazio Nicolotti, Serge Thorimbert and Michèle Salmain

Eur J Inorg Chem, 2017, 2017, 3622
DOI: 10.1002/ejic.201700365

Enantioselective Synthesis of Sulfoxides: 2000−2009

Elżbieta Wojaczyńska and Jacek Wojaczyński

Chem. Rev., 2010, 110, 4303
DOI: 10.1021/cr900147h

The Outer-Coordination Sphere: Incorporating Amino Acids and Peptides as Ligands for Homogeneous Catalysts to Mimic Enzyme Function

Wendy J. Shaw

Catalysis Reviews, 2012, 54, 489
DOI: 10.1080/01614940.2012.679453

Transition metal salen complexes in bioinorganic and medicinal chemistry

Andrea Erxleben

Inorganica Chimica Acta, 2018, 472, 40
DOI: 10.1016/j.ica.2017.06.060

Metal-catalyzed asymmetric sulfoxidation, epoxidation and hydroxylation by hydrogen peroxide

Hassan Srour, Paul Le Maux, Soizic Chevance and Gérard Simonneaux

Coordination Chemistry Reviews, 2013, 257, 3030
DOI: 10.1016/j.ccr.2013.05.010

Artificial Metalloenzymes: Reaction Scope and Optimization Strategies

Fabian Schwizer, Yasunori Okamoto, Tillmann Heinisch, Yifan Gu, Michela M. Pellizzoni, Vincent Lebrun, Raphael Reuter, Valentin Köhler, Jared C. Lewis and Thomas R. Ward

Chem. Rev., 2018, 118, 142
DOI: 10.1021/acs.chemrev.7b00014

Chiral Wide-Bite-Angle Diphosphine Ligands: Synthesis, Coordination Chemistry, and Application in Pd-Catalyzed Allylic Alkylation

Christine F. Czauderna, Amanda G. Jarvis, Frank J. L. Heutz, David B. Cordes, Alexandra M. Z. Slawin, Jarl Ivar van der Vlugt and Paul C. J. Kamer

Organometallics, 2015, 34, 1608
DOI: 10.1021/om5008055

Artificial Metalloenzymes

Fiora Rosati and Gerard Roelfes

ChemCatChem, 2010, 2, 916
DOI: 10.1002/cctc.201000011

The Protein Environment Drives Selectivity for Sulfide Oxidation by an Artificial Metalloenzyme

Pierre Rousselot‐Pailley, Constance Bochot, Caroline Marchi‐Delapierre, Adeline Jorge‐Robin, Lydie Martin, Juan C. Fontecilla‐Camps, Christine Cavazza and Stéphane Ménage

ChemBioChem, 2009, 10, 545
DOI: 10.1002/cbic.200800595

Design of functional metalloproteins

Yi Lu, Natasha Yeung, Nathan Sieracki and Nicholas M. Marshall

Nature, 2009, 460, 855
DOI: 10.1038/nature08304

Introducing Metallosalens into Biological Studies: The Renaissance of Traditional Coordination Complexes

Hao‐Yan Yin, Juan Tang and Jun‐Long Zhang

Eur J Inorg Chem, 2017, 2017, 5085
DOI: 10.1002/ejic.201700695

Protein Design: Toward Functional Metalloenzymes

Fangting Yu, Virginia M. Cangelosi, Melissa L. Zastrow, Matteo Tegoni, Jefferson S. Plegaria, Alison G. Tebo, Catherine S. Mocny, Leela Ruckthong, Hira Qayyum and Vincent L. Pecoraro

Chem. Rev., 2014, 114, 3495
DOI: 10.1021/cr400458x

Catalyst design in oxidation chemistry; from KMnO4 to artificial metalloenzymes

Megan V. Doble, Andrew C.C. Ward, Peter J. Deuss, Amanda G. Jarvis and Paul C.J. Kamer

Bioorganic & Medicinal Chemistry, 2014, 22, 5657
DOI: 10.1016/j.bmc.2014.07.002

Artificial enzymes with protein scaffolds: Structural design and modification

Takashi Matsuo and Shun Hirota

Bioorganic & Medicinal Chemistry, 2014, 22, 5638
DOI: 10.1016/j.bmc.2014.06.021

Ring‐Closing and Cross‐Metathesis with Artificial Metalloenzymes Created by Covalent Active Site‐Directed Hybridization of a Lipase

Manuel Basauri‐Molina, Dide G. A. Verhoeven, Arnoldus J. van Schaik, Henk Kleijn and Robertus J. M. Klein Gebbink

Chemistry A European J, 2015, 21, 15676
DOI: 10.1002/chem.201502381

Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere

Casey Van Stappen, Yunling Deng, Yiwei Liu, Hirbod Heidari, Jing-Xiang Wang, Yu Zhou, Aaron P. Ledray and Yi Lu

Chem. Rev., 2022, 122, 11974
DOI: 10.1021/acs.chemrev.2c00106

Artificial Metalloenzymes and Metallopeptide Catalysts for Organic Synthesis

Jared C. Lewis

ACS Catal., 2013, 3, 2954
DOI: 10.1021/cs400806a

Understanding and Modulating Metalloenzymes with Unnatural Amino Acids, Non-Native Metal Ions, and Non-Native Metallocofactors

Evan N. Mirts, Ambika Bhagi-Damodaran and Yi Lu

Acc. Chem. Res., 2019, 52, 935
DOI: 10.1021/acs.accounts.9b00011