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For: Sheng X, Kazemi M, Planas F, Himo F. Modeling Enzymatic Enantioselectivity using Quantum Chemical Methodology. ACS Catal 2020;10:6430-49. [DOI: 10.1021/acscatal.0c00983] [Cited by in Crossref: 34] [Cited by in F6Publishing: 24] [Article Influence: 17.0] [Reference Citation Analysis]
Number Citing Articles
1 Winkler CK, Schrittwieser JH, Kroutil W. Power of Biocatalysis for Organic Synthesis. ACS Cent Sci 2021;7:55-71. [PMID: 33532569 DOI: 10.1021/acscentsci.0c01496] [Cited by in Crossref: 65] [Cited by in F6Publishing: 40] [Article Influence: 65.0] [Reference Citation Analysis]
2 Sheng X, Himo F. Mechanism of 3‐Methylglutaconyl CoA Decarboxylase AibA/AibB: Pericyclic Reaction versus Direct Decarboxylation. Angew Chem 2020;132:23173-7. [DOI: 10.1002/ange.202008919] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
3 Planas F, Mcleish MJ, Himo F. Enzymatic Stetter Reaction: Computational Study of the Reaction Mechanism of MenD. ACS Catal 2021;11:12355-66. [DOI: 10.1021/acscatal.1c02292] [Cited by in Crossref: 2] [Article Influence: 2.0] [Reference Citation Analysis]
4 Ali HS, Henchman RH, Visser SP. Mechanism of Oxidative Ring‐Closure as Part of the Hygromycin Biosynthesis Step by a Nonheme Iron Dioxygenase. ChemCatChem 2021;13:3054-66. [DOI: 10.1002/cctc.202100393] [Cited by in Crossref: 3] [Cited by in F6Publishing: 1] [Article Influence: 3.0] [Reference Citation Analysis]
5 Dong Y, Li T, Zhang S, Sanchis J, Yin H, Ren J, Sheng X, Li G, Reetz MT. Biocatalytic Baeyer–Villiger Reactions: Uncovering the Source of Regioselectivity at Each Evolutionary Stage of a Mutant with Scrutiny of Fleeting Chiral Intermediates. ACS Catal 2022;12:3669-80. [DOI: 10.1021/acscatal.2c00415] [Reference Citation Analysis]
6 Liu N, Wu L, Feng J, Sheng X, Li J, Chen X, Li J, Liu W, Zhou J, Wu Q, Zhu D. Crystal Structures and Catalytic Mechanism of l-erythro-3,5-Diaminohexanoate Dehydrogenase and Rational Engineering for Asymmetric Synthesis of β-Amino Acids. Angew Chem Int Ed Engl 2021;60:10203-10. [PMID: 33624917 DOI: 10.1002/anie.202017225] [Reference Citation Analysis]
7 Sheng X, Himo F. Computational Study of Pictet–Spenglerase Strictosidine Synthase: Reaction Mechanism and Origins of Enantioselectivity of Natural and Non-Natural Substrates. ACS Catal 2020;10:13630-40. [DOI: 10.1021/acscatal.0c03758] [Cited by in Crossref: 9] [Cited by in F6Publishing: 8] [Article Influence: 4.5] [Reference Citation Analysis]
8 Prejanò M, Sheng X, Himo F. Computational Study of Mechanism and Enantioselectivity of Imine Reductase from Amycolatopsis orientalis. ChemistryOpen 2021. [PMID: 34825518 DOI: 10.1002/open.202100250] [Reference Citation Analysis]
9 Blakemore CA, France SP, Samp L, Nason DM, Yang E, Howard RM, Coffman KJ, Yang Q, Smith AC, Evrard E, Li W, Dai L, Yang L, Chen Z, Zhang Q, He F, Zhang J. Scalable, Telescoped Hydrogenolysis–Enzymatic Decarboxylation Process for the Asymmetric Synthesis of ( R )-α-Heteroaryl Propionic Acids. Org Process Res Dev 2021;25:421-6. [DOI: 10.1021/acs.oprd.0c00397] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
10 Himo F, de Visser SP. Status report on the quantum chemical cluster approach for modeling enzyme reactions. Commun Chem 2022;5. [DOI: 10.1038/s42004-022-00642-2] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
11 Liu X, Yuan Z, Su H, Hou X, Deng Z, Xu H, Guo B, Yin D, Sheng X, Rao Y. Molecular Basis of the Unusual Seven-Membered Methylenedioxy Bridge Formation Catalyzed by Fe(II)/α-KG-Dependent Oxygenase CTB9. ACS Catal 2022;12:3689-99. [DOI: 10.1021/acscatal.1c04627] [Reference Citation Analysis]
12 Liu H, Panjikar S, Sheng X, Futamura Y, Zhang C, Shao N, Osada H, Zou H. β-Methyltryptamine Provoking the Crucial Role of Strictosidine Synthase Tyr151-OH for Its Stereoselective Pictet-Spengler Reactions to Tryptoline-type Alkaloids. ACS Chem Biol 2022;17:187-97. [PMID: 34994203 DOI: 10.1021/acschembio.1c00844] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
13 Sánchez-Aparicio JE, Sciortino G, Mates-Torres E, Lledós A, Maréchal JD. Successes and challenges in multiscale modelling of artificial metalloenzymes: the case study of POP-Rh2 cyclopropanase. Faraday Discuss 2022. [PMID: 35147145 DOI: 10.1039/d1fd00069a] [Reference Citation Analysis]
14 Kapon Y, Saha A, Duanis-assaf T, Stuyver T, Ziv A, Metzger T, Yochelis S, Shaik S, Naaman R, Reches M, Paltiel Y. Evidence for new enantiospecific interaction force in chiral biomolecules. Chem 2021;7:2787-99. [DOI: 10.1016/j.chempr.2021.08.002] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
15 Bím D, Navrátil M, Gutten O, Konvalinka J, Kutil Z, Culka M, Navrátil V, Alexandrova AN, Bařinka C, Rulíšek L. Predicting Effects of Site-Directed Mutagenesis on Enzyme Kinetics by QM/MM and QM Calculations: A Case of Glutamate Carboxypeptidase II. J Phys Chem B 2022;126:132-43. [PMID: 34978450 DOI: 10.1021/acs.jpcb.1c09240] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
16 de Visser SP, Lin Y, Ali HS, Bagha UK, Mukherjee G, Sastri CV. Negative catalysis / non-Bell-Evans-Polanyi reactivity by metalloenzymes: Examples from mononuclear heme and non-heme iron oxygenases. Coordination Chemistry Reviews 2021;439:213914. [DOI: 10.1016/j.ccr.2021.213914] [Cited by in Crossref: 4] [Cited by in F6Publishing: 1] [Article Influence: 4.0] [Reference Citation Analysis]
17 Lin YT, Ali HS, de Visser SP. Electrostatic Perturbations from the Protein Affect C-H Bond Strengths of the Substrate and Enable Negative Catalysis in the TmpA Biosynthesis Enzyme. Chemistry 2021;27:8851-64. [PMID: 33978257 DOI: 10.1002/chem.202100791] [Cited by in Crossref: 4] [Cited by in F6Publishing: 2] [Article Influence: 4.0] [Reference Citation Analysis]
18 Han SB, Ali HS, de Visser SP. Glutarate Hydroxylation by the Carbon Starvation-Induced Protein D: A Computational Study into the Stereo- and Regioselectivities of the Reaction. Inorg Chem 2021;60:4800-15. [DOI: 10.1021/acs.inorgchem.0c03749] [Cited by in Crossref: 4] [Cited by in F6Publishing: 2] [Article Influence: 4.0] [Reference Citation Analysis]
19 Wu L, Qin L, Nie Y, Xu Y, Zhao YL. Computer-aided understanding and engineering of enzymatic selectivity. Biotechnol Adv 2021;:107793. [PMID: 34217814 DOI: 10.1016/j.biotechadv.2021.107793] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 2.0] [Reference Citation Analysis]
20 Sun X, Du J, Tan J, Zhan S. A mono-oxo-bridged binuclear iron( iii ) complex with a Fe–O–Fe angle of 180.0° and its catalytic activity for hydrogen evolution. New J Chem . [DOI: 10.1039/d1nj05904a] [Reference Citation Analysis]
21 Ding Y, Cui K, Liu X, Xie Q, Guo Z, Chen Y. Lignin peroxidase-catalyzed direct oxidation of trace organic pollutants through a long-range electron transfer mechanism: Using propranolol as an example. Journal of Hazardous Materials 2022;431:128544. [DOI: 10.1016/j.jhazmat.2022.128544] [Reference Citation Analysis]
22 Zumwalt L, Perkins A, Ogba OM. Mechanism and Chemoselectivity for HOCl-Mediated Oxidation of Zinc-Bound Thiolates. Chemphyschem 2020;21:2384-7. [PMID: 32915482 DOI: 10.1002/cphc.202000634] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
23 Zhou J, Xu G, Ni Y. Stereochemistry in Asymmetric Reduction of Bulky–Bulky Ketones by Alcohol Dehydrogenases. ACS Catal 2020;10:10954-66. [DOI: 10.1021/acscatal.0c02646] [Cited by in Crossref: 16] [Cited by in F6Publishing: 8] [Article Influence: 8.0] [Reference Citation Analysis]
24 Ali HS, Henchman RH, Warwicker J, de Visser SP. How Do Electrostatic Perturbations of the Protein Affect the Bifurcation Pathways of Substrate Hydroxylation versus Desaturation in the Nonheme Iron-Dependent Viomycin Biosynthesis Enzyme? J Phys Chem A 2021;125:1720-37. [DOI: 10.1021/acs.jpca.1c00141] [Cited by in Crossref: 7] [Cited by in F6Publishing: 5] [Article Influence: 7.0] [Reference Citation Analysis]