| Year |
Citation |
Score |
| 2023 |
Zhang Y, Mokkawes T, de Visser SP. Insights into Cytochrome P450 Enzymes Catalyzed Defluorination of Aromatic Fluorides. Angewandte Chemie (International Ed. in English). e202310785. PMID 37641517 DOI: 10.1002/anie.202310785 |
0.364 |
|
| 2023 |
Cao Y, Valdez-Moreira JA, Hay S, Smith JM, de Visser SP, de Visser SP. Reactivity Differences of Trigonal Pyramidal Nonheme Iron(IV)-Oxo and Iron(III)-Oxo Complexes: Experiment and Theory. Chemistry (Weinheim An Der Bergstrasse, Germany). e202300271. PMID 37159057 DOI: 10.1002/chem.202300271 |
0.359 |
|
| 2023 |
Bagha UK, Yadav R, Mokkawes T, Satpathy JK, Kumar D, Sastri CV, de Visser SP. Defluorination of fluorophenols by a nonheme iron(IV)-oxo species: observation of a new intermediate along the reaction. Chemistry (Weinheim An Der Bergstrasse, Germany). e202300478. PMID 37066848 DOI: 10.1002/chem.202300478 |
0.329 |
|
| 2023 |
Hermano Sampaio Dias A, Yadav R, Mokkawes T, Kumar A, Skaf MS, Sastri CV, Kumar D, de Visser SP. Biotransformation of Bisphenol by Human Cytochrome P450 2C9 Enzymes: A Density Functional Theory Study. Inorganic Chemistry. PMID 36651185 DOI: 10.1021/acs.inorgchem.2c03984 |
0.369 |
|
| 2022 |
Dixit VA, Murty US, Bajaj P, Blumberger J, de Visser SP. Mechanisms of Electron Transfer Rate Modulations in Cytochrome P450 BM3. The Journal of Physical Chemistry. B. PMID 36384294 DOI: 10.1021/acs.jpcb.2c03967 |
0.747 |
|
| 2022 |
Mokkawes T, Lim ZQ, de Visser SP. Mechanism of Melatonin Metabolism by CYP1A1: What Determines the Bifurcation Pathways of Hydroxylation versus Deformylation? The Journal of Physical Chemistry. B. 126: 9591-9606. PMID 36380557 DOI: 10.1021/acs.jpcb.2c07200 |
0.336 |
|
| 2022 |
Gérard EF, Yadav V, Goldberg DP, de Visser SP. What Drives Radical Halogenation versus Hydroxylation in Mononuclear Nonheme Iron Complexes? A Combined Experimental and Computational Study. Journal of the American Chemical Society. PMID 35537044 DOI: 10.1021/jacs.2c01375 |
0.309 |
|
| 2022 |
Yeh CG, Mokkawes T, Bradley JM, Le Brun NE, de Visser SP. Second Coordination Sphere Effects on the Mechanistic Pathways for Dioxygen Activation by a Ferritin: Involvement of a Tyr Radical and the Identification of a Cation Binding Site. Chembiochem : a European Journal of Chemical Biology. e202200257. PMID 35510795 DOI: 10.1002/cbic.202200257 |
0.333 |
|
| 2022 |
Matsumura H, Faponle AS, Hagedoorn PL, Tosha T, de Visser SP, Moënne-Loccoz P. Mechanism of substrate inhibition in cytochrome-c dependent NO reductases from denitrifying bacteria (cNORs). Journal of Inorganic Biochemistry. 231: 111781. PMID 35259597 DOI: 10.1016/j.jinorgbio.2022.111781 |
0.305 |
|
| 2022 |
Bagha UK, Satpathy JK, Mukherjee G, Barman P, Kumar D, de Visser SP, Sastri CV. Oxidative dehalogenation of halophenols by high-valent nonheme iron(IV)-oxo intermediates. Faraday Discussions. PMID 35170590 DOI: 10.1039/d1fd00064k |
0.377 |
|
| 2021 |
Ortmayer M, Hardy FJ, Quesne MG, Fisher K, Levy C, Heyes DJ, Catlow CRA, de Visser SP, Rigby SEJ, Hay S, Green AP. A Noncanonical Tryptophan Analogue Reveals an Active Site Hydrogen Bond Controlling Ferryl Reactivity in a Heme Peroxidase. Jacs Au. 1: 913-918. PMID 34337604 DOI: 10.1021/jacsau.1c00145 |
0.701 |
|
| 2021 |
Latifi R, Palluccio TD, Ye W, Minnick JL, Glinton KS, Rybak-Akimova EV, de Visser SP, Tahsini L. pH Changes That Induce an Axial Ligand Effect on Nonheme Iron(IV) Oxo Complexes with an Appended Aminopropyl Functionality. Inorganic Chemistry. PMID 34291939 DOI: 10.1021/acs.inorgchem.1c01312 |
0.302 |
|
| 2021 |
Lin YT, de Visser SP. Product Distributions of Cytochrome P450 OleT with Phenyl-Substituted Fatty Acids: A Computational Study. International Journal of Molecular Sciences. 22. PMID 34281222 DOI: 10.3390/ijms22137172 |
0.306 |
|
| 2021 |
Lin YT, de Visser SP. Product Distributions of Cytochrome P450 OleT with Phenyl-Substituted Fatty Acids: A Computational Study. International Journal of Molecular Sciences. 22. PMID 34281222 DOI: 10.3390/ijms22137172 |
0.306 |
|
| 2021 |
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. Inorganic Chemistry. PMID 33764783 DOI: 10.1021/acs.inorgchem.0c03749 |
0.344 |
|
| 2021 |
Chen X, Sun D, Gao L, Zhao Y, de Visser SP, Wang Y. Theoretical studies unveil the unusual bonding in oxygenation reactions involving cobalt(II)-iodylarene complexes. Chemical Communications (Cambridge, England). PMID 33630000 DOI: 10.1039/d0cc07894h |
0.378 |
|
| 2020 |
Chowdhury AS, Ali HS, Faponle AS, de Visser SP. How external perturbations affect the chemoselectivity of substrate activation by cytochrome P450 OleT. Physical Chemistry Chemical Physics : Pccp. PMID 33226036 DOI: 10.1039/d0cp05169a |
0.336 |
|
| 2020 |
Lee CWZ, Mubarak MQE, Green AP, de Visser SP. How Does Replacement of the Axial Histidine Ligand in Cytochrome Peroxidase by N-Methyl Histidine Affect Its Properties and Functions? A Computational Study. International Journal of Molecular Sciences. 21. PMID 32992593 DOI: 10.3390/ijms21197133 |
0.31 |
|
| 2020 |
de Visser S, Ali HS, Henchman RH. What determines the selectivity of arginine dihydroxylation by the nonheme iron enzyme OrfP? Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 32965733 DOI: 10.1002/chem.202004019 |
0.309 |
|
| 2020 |
Louka S, Barry SM, Heyes DJ, Mubarak MQE, Ali HS, Alkhalaf LM, Munro AW, Scrutton NS, Challis GL, de Visser SP. Catalytic Mechanism of Aromatic Nitration by Cytochrome P450 TxtE: Involvement of a Ferric-Peroxynitrite Intermediate. Journal of the American Chemical Society. PMID 32811149 DOI: 10.1021/jacs.0c05070 |
0.387 |
|
| 2020 |
Dixit VA, Warwicker J, de Visser SP. How Do Metal Ions Modulate the Rate-Determining Electron-Transfer Step in Cytochrome P450 Reactions? Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 32761661 DOI: 10.1002/chem.202003024 |
0.75 |
|
| 2020 |
Ali HS, Henchman R, de Visser S. Lignin biodegradation by a cytochrome P450 enzyme: A computational study into syringol activation by GcoA. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 32613677 DOI: 10.1002/Chem.202002203 |
0.336 |
|
| 2020 |
Reinhard FGC, Lin YT, Stańczak A, de Visser SP. Bioengineering of Cytochrome P450 OleT: How Does Substrate Positioning Affect the Product Distributions? Molecules (Basel, Switzerland). 25. PMID 32526971 DOI: 10.3390/molecules25112675 |
0.312 |
|
| 2020 |
Ali HS, Henchman RH, de Visser SP. Cross-linking of aromatic phenolate groups by cytochrome P450 enzymes: a model for the biosynthesis of vancomycin by OxyB. Organic & Biomolecular Chemistry. PMID 32515757 DOI: 10.1039/D0Ob01023E |
0.343 |
|
| 2020 |
Mukherjee G, Reinhard FGC, Bagha UK, Sastri CV, de Visser SP. Sluggish reactivity by a nonheme iron(iv)-tosylimido complex as compared to its oxo analogue. Dalton Transactions (Cambridge, England : 2003). PMID 32314764 DOI: 10.1039/D0Dt00018C |
0.344 |
|
| 2020 |
Latifi R, Minnick JL, Quesne MG, de Visser SP, Tahsini L. Computational studies of DNA base repair mechanisms by nonheme iron dioxygenases: selective epoxidation and hydroxylation pathways. Dalton Transactions (Cambridge, England : 2003). PMID 32141456 DOI: 10.1039/D0Dt00007H |
0.689 |
|
| 2019 |
Zaragoza JPT, Cummins DC, Mubarak MQE, Siegler MA, de Visser SP, Goldberg DP. Hydrogen Atom Abstraction by High-Valent Fe(OH) versus Mn(OH) Porphyrinoid Complexes: Mechanistic Insights from Experimental and Computational Studies. Inorganic Chemistry. PMID 31804814 DOI: 10.1021/Acs.Inorgchem.9B02923 |
0.364 |
|
| 2019 |
de Visser SP. Second-Coordination Sphere Effects on Selectivity and Specificity of Heme and Nonheme Iron Enzymes. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 31804749 DOI: 10.1002/chem.201905119 |
0.314 |
|
| 2019 |
Ghafoor S, Mansha A, de Visser SP. Selective hydrogen atom abstraction from dihydroflavonol is the key step in the flavonol synthesis enzyme and avoids by-products. Journal of the American Chemical Society. PMID 31749356 DOI: 10.1021/jacs.9b10526 |
0.304 |
|
| 2019 |
Mubarak MQE, de Visser SP. Second-Coordination Sphere Effect on the Reactivity of Vanadium-Peroxo Complexes: A Computational Study. Inorganic Chemistry. PMID 31721569 DOI: 10.1021/acs.inorgchem.9b01778 |
0.323 |
|
| 2019 |
Mubarak MQE, de Visser SP. Reactivity patterns of vanadium(iv/v)-oxo complexes with olefins in the presence of peroxides: a computational study. Dalton Transactions (Cambridge, England : 2003). PMID 31670737 DOI: 10.1039/c9dt03048d |
0.3 |
|
| 2019 |
Lin YT, Stańczak A, Manchev Y, Straganz G, de Visser S. Can a mononuclear iron(III)-superoxo active site catalyze the decarboxylation of dodecanoic acid in UndA to produce biofuels? Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 31584704 DOI: 10.1002/chem.201903783 |
0.308 |
|
| 2019 |
Mubarak MQE, Sorokin AB, de Visser SP. Properties and reactivity of μ-nitrido-bridged dimetal porphyrinoid complexes: how does ruthenium compare to iron? Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 31560098 DOI: 10.1007/s00775-019-01725-7 |
0.377 |
|
| 2019 |
de Visser S, Tobing A, Mukherjee G, Colomban C, Sastri C, Sorokin A. Mechanism of Oxidative Activation of Fluorinated Aromatic Compounds by N-Bridged Diiron-Phthalocyanine. What determines the reactivity? Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 31339185 DOI: 10.1002/Chem.201902934 |
0.348 |
|
| 2019 |
Pangia TM, Yadav V, Gérard EF, Lin YT, de Visser SP, Jameson GNL, Goldberg DP. Mechanistic Investigation of Oxygen Rebound in a Mononuclear Nonheme Iron Complex. Inorganic Chemistry. PMID 31313577 DOI: 10.1021/Acs.Inorgchem.9B01208 |
0.326 |
|
| 2019 |
Davethu PA, de Visser SP. CO Reduction on an Iron-Porphyrin Center: A Computational Study. The Journal of Physical Chemistry. A. PMID 31283234 DOI: 10.1021/acs.jpca.9b05102 |
0.308 |
|
| 2019 |
Zeb N, Rashid MH, Mubarak MQE, Ghafoor S, de Visser SP. Flavonol biosynthesis by nonheme iron dioxygenases: A computational study into the structure and mechanism. Journal of Inorganic Biochemistry. 198: 110728. PMID 31203088 DOI: 10.1016/j.jinorgbio.2019.110728 |
0.357 |
|
| 2019 |
Barman P, Cantu Reinhard F, Bagha UK, Kumar D, Sastri C, de Visser S. Hydrogen by Deuterium Substitution in an Aldehyde Tunes the Regioselectivity by a Nonheme Manganese(III)-Peroxo Complex. Angewandte Chemie (International Ed. in English). PMID 31108009 DOI: 10.1002/Anie.201905416 |
0.309 |
|
| 2019 |
Khan FST, Shah SJ, Bhowmik S, Reinhard FGC, Sainna MA, de Visser SP, Rath SP. Equatorial ligand plane perturbations lead to a spin-state change in an iron(iii) porphyrin dimer. Dalton Transactions (Cambridge, England : 2003). PMID 30994665 DOI: 10.1039/C9Dt01182J |
0.777 |
|
| 2019 |
de Visser S, Pattanayak S, Cantu Reinhard F, Rana A, Gupta SS. The equatorial ligand effect on the properties and reactivity of iron(V)-oxo intermediates. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 30912866 DOI: 10.1002/Chem.201900708 |
0.331 |
|
| 2019 |
de Visser S, Mukherjee G, Kumar D, Sastri C, Alili A, Barman P. Interplay Between Steric and Electronic Effects: A Joint Spectroscopy and Computational Study of Nonheme Iron(IV)-oxo Complexes. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 30720909 DOI: 10.1002/Chem.201806430 |
0.333 |
|
| 2018 |
Timmins A, Fowler NJ, Warwicker J, Straganz GD, de Visser SP. Does Substrate Positioning Affect the Selectivity and Reactivity in the Hectochlorin Biosynthesis Halogenase? Frontiers in Chemistry. 6: 513. PMID 30425979 DOI: 10.3389/fchem.2018.00513 |
0.306 |
|
| 2018 |
Cantú Reinhard FG, DuBois J, de Visser SP. Catalytic Mechanism of Nogalamycin Monoxygenase: How Does Nature Synthesize Antibiotics Without a Metal Cofactor? The Journal of Physical Chemistry. B. PMID 30388008 DOI: 10.1021/acs.jpcb.8b09648 |
0.347 |
|
| 2018 |
Mukherjee G, Lee CWZ, Nag SS, Alili A, Cantú Reinhard FG, Kumar D, Sastri CV, de Visser SP. Dramatic rate-enhancement of oxygen atom transfer by an iron(iv)-oxo species by equatorial ligand field perturbations. Dalton Transactions (Cambridge, England : 2003). PMID 30259028 DOI: 10.1039/C8Dt02142B |
0.313 |
|
| 2018 |
Postils V, Saint-André M, Timmins A, Li XX, Wang Y, Luis JM, Solà M, de Visser SP. Quantum Mechanics/Molecular Mechanics Studies on the Relative Reactivities of Compound I and II in Cytochrome P450 Enzymes. International Journal of Molecular Sciences. 19. PMID 29986417 DOI: 10.3390/Ijms19071974 |
0.408 |
|
| 2018 |
de Visser SP. Mechanistic Insight on the Activity and Substrate Selectivity of Nonheme Iron Dioxygenases. Chemical Record (New York, N.Y.). PMID 29878456 DOI: 10.1002/tcr.201800033 |
0.323 |
|
| 2017 |
Kaczmarek MA, Malhotra A, Balan GA, Timmins A, de Visser SP. Nitrogen Reduction to Ammonia on a Biomimetic Mononuclear Iron Centre: Insights into the Nitrogenase Enzyme. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 29165842 DOI: 10.1002/chem.201704688 |
0.353 |
|
| 2017 |
Kaczmarek MA, Malhotra A, Balan GA, Timmins A, de Visser SP. Nitrogen Reduction to Ammonia on a Biomimetic Mononuclear Iron Centre: Insights into the Nitrogenase Enzyme. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 29165842 DOI: 10.1002/chem.201704688 |
0.353 |
|
| 2017 |
Cantú Reinhard FG, Barman P, Mukherjee G, Kumar J, Kumar D, Kumar D, Sastri CV, de Visser SP. Keto-enol tautomerization triggers an electrophilic aldehyde deformylation reaction by a nonheme manganese(III)-peroxo complex. Journal of the American Chemical Society. PMID 29148746 DOI: 10.1021/Jacs.7B10033 |
0.329 |
|
| 2017 |
Faponle AS, Seebeck FP, de Visser SP. Sulfoxide synthase versus cysteine dioxygenase reactivity in a nonheme iron enzyme. Journal of the American Chemical Society. PMID 28602090 DOI: 10.1021/jacs.7b04251 |
0.367 |
|
| 2017 |
de Visser S, Li XX, Postils V, Sun W, Faponle A, Sola M, Wang Y, Nam W. Reactivity patterns of protonated Compound II and Compound I of Cytochrome P450: What is the better oxidant? Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 28295741 DOI: 10.1002/Chem.201700363 |
0.344 |
|
| 2017 |
Cantú Reinhard FG, de Visser SP. Oxygen Atom Transfer Using an Iron(IV)-Oxo Embedded in a Tetracyclic N-Heterocyclic Carbene System: How Does the Reactivity Compare to Cytochrome P450 Compound I? Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 28052598 DOI: 10.1002/chem.201605505 |
0.377 |
|
| 2016 |
Cantú Reinhard FG, Faponle AS, de Visser SP. Substrate Sulfoxidation by an Iron(IV)-Oxo Complex: Benchmarking Computationally Calculated Barrier Heights to Experiment. The Journal of Physical Chemistry. A. 120: 9805-9814. PMID 27973805 DOI: 10.1021/acs.jpca.6b09765 |
0.308 |
|
| 2016 |
Cantu Reinhard F, Sainna M, Upadhayay P, Balan A, Kumar D, Fornarini S, Crestoni ME, de Visser S. A systematic account on aromatic hydroxylation by a cytochrome P450 model Compound I: A low-pressure mass spectrometry and computational study. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 27727524 DOI: 10.1002/Chem.201604361 |
0.796 |
|
| 2016 |
Barman P, Faponle AS, Vardhaman AK, Angelone D, Löhr AM, Browne WR, Comba P, Sastri CV, de Visser SP. Influence of Ligand Architecture in Tuning Reaction Bifurcation Pathways for Chlorite Oxidation by Non-Heme Iron Complexes. Inorganic Chemistry. PMID 27704794 DOI: 10.1021/Acs.Inorgchem.6B01384 |
0.362 |
|
| 2016 |
Yang T, Quesne MG, Neu HM, Cantú Reinhard FG, Goldberg DP, de Visser SP. Singlet versus Triplet Reactivity in an Mn(V)-Oxo Species: Testing Theoretical Predictions Against Experimental Evidence. Journal of the American Chemical Society. PMID 27545752 DOI: 10.1021/Jacs.6B05027 |
0.705 |
|
| 2016 |
Tchesnokov EP, Faponle AS, Davies CG, Quesne MG, Turner R, Fellner M, Souness RJ, Wilbanks SM, de Visser SP, Jameson GN. An iron-oxygen intermediate formed during the catalytic cycle of cysteine dioxygenase. Chemical Communications (Cambridge, England). PMID 27297454 DOI: 10.1039/C6Cc03904A |
0.681 |
|
| 2016 |
Faponle AS, Banse F, de Visser SP. Arene activation by a nonheme iron(III)-hydroperoxo complex: pathways leading to phenol and ketone products. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 27099221 DOI: 10.1007/s00775-016-1354-y |
0.329 |
|
| 2016 |
Faponle AS, Quesne MG, de Visser SP. Origin of the Regioselective Fatty-Acid Hydroxylation versus Decarboxylation by a Cytochrome P450 Peroxygenase: What Drives the Reaction to Biofuel Production? Chemistry (Weinheim An Der Bergstrasse, Germany). 22: 5478-83. PMID 26918676 DOI: 10.1002/Chem.201600739 |
0.688 |
|
| 2015 |
İşci Ü, Faponle AS, Afanasiev P, Albrieux F, Briois V, Ahsen V, Dumoulin F, Sorokin AB, de Visser SP. Site-selective formation of an iron(iv)-oxo species at the more electron-rich iron atom of heteroleptic μ-nitrido diiron phthalocyanines. Chemical Science. 6: 5063-5075. PMID 30155008 DOI: 10.1039/c5sc01811k |
0.336 |
|
| 2015 |
Sainna MA, Kumar S, Kumar D, Fornarini S, Crestoni ME, de Visser SP. A comprehensive test set of epoxidation rate constants for iron(iv)-oxo porphyrin cation radical complexes. Chemical Science. 6: 1516-1529. PMID 29560240 DOI: 10.1039/C4Sc02717E |
0.802 |
|
| 2015 |
Draksharapu A, Angelone D, Quesne MG, Padamati SK, Gómez L, Hage R, Costas M, Browne WR, de Visser SP. Identification and Spectroscopic Characterization of Nonheme Iron(III) Hypochlorite Intermediates. Angewandte Chemie (Weinheim An Der Bergstrasse, Germany). 127: 4431-4435. PMID 27478260 DOI: 10.1002/ange.201411995 |
0.686 |
|
| 2015 |
Quesne MG, Borowski T, de Visser SP. Quantum Mechanics/Molecular Mechanics Modeling of Enzymatic Processes: Caveats and Breakthroughs. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 26696271 DOI: 10.1002/Chem.201503802 |
0.648 |
|
| 2015 |
Sainna MA, de Visser SP. Alkyl Chain Growth on a Transition Metal Center: How Does Iron Compare to Ruthenium and Osmium? International Journal of Molecular Sciences. 16: 23369-81. PMID 26426009 DOI: 10.3390/Ijms161023369 |
0.773 |
|
| 2015 |
Sahoo D, Quesne MG, de Visser SP, Rath SP. Hydrogen-Bonding Interactions Trigger a Spin-Flip in Iron(III) Porphyrin Complexes. Angewandte Chemie (Weinheim An Der Bergstrasse, Germany). 127: 4878-4882. PMID 26109743 DOI: 10.1002/Ange.201411399 |
0.72 |
|
| 2015 |
Hernández-Ortega A, Quesne MG, Bui S, Heyes DJ, Steiner RA, Scrutton NS, de Visser SP. Catalytic mechanism of cofactor-free dioxygenases and how they circumvent spin-forbidden oxygenation of their substrates. Journal of the American Chemical Society. 137: 7474-87. PMID 25988744 DOI: 10.1021/Jacs.5B03836 |
0.718 |
|
| 2015 |
Ji L, Faponle AS, Quesne MG, Sainna MA, Zhang J, Franke A, Kumar D, van Eldik R, Liu W, de Visser SP. Drug metabolism by cytochrome p450 enzymes: what distinguishes the pathways leading to substrate hydroxylation over desaturation? Chemistry (Weinheim An Der Bergstrasse, Germany). 21: 9083-92. PMID 25924594 DOI: 10.1002/Chem.201500329 |
0.808 |
|
| 2015 |
Draksharapu A, Angelone D, Quesne MG, Padamati SK, Gómez L, Hage R, Costas M, Browne WR, de Visser SP. Identification and spectroscopic characterization of nonheme iron(III) hypochlorite intermediates. Angewandte Chemie (International Ed. in English). 54: 4357-61. PMID 25663379 DOI: 10.1002/Anie.201411995 |
0.686 |
|
| 2015 |
Sahoo D, Quesne MG, de Visser SP, Rath SP. Hydrogen-bonding interactions trigger a spin-flip in iron(III) porphyrin complexes. Angewandte Chemie (International Ed. in English). 54: 4796-800. PMID 25645603 DOI: 10.1002/anie.201411399 |
0.72 |
|
| 2015 |
Sainna MA, Sil D, Sahoo D, Martin B, Rath SP, Comba P, de Visser SP. Spin-state ordering in hydroxo-bridged diiron(III)bisporphyrin complexes. Inorganic Chemistry. 54: 1919-30. PMID 25610949 DOI: 10.1021/Ic502803B |
0.775 |
|
| 2015 |
Faponle AS, Quesne MG, Sastri CV, Banse F, de Visser SP. Differences and comparisons of the properties and reactivities of iron(III)-hydroperoxo complexes with saturated coordination sphere. Chemistry (Weinheim An Der Bergstrasse, Germany). 21: 1221-36. PMID 25399782 DOI: 10.1002/Chem.201404918 |
0.729 |
|
| 2015 |
Sainna MA, Singh D, Kumar D, De Visser SP. A trimetal carbene with reactivity reminiscent of fischer-tropsch catalysis Organometallics. 34: 1651-1660. DOI: 10.1021/Acs.Organomet.5B00305 |
0.774 |
|
| 2015 |
Faponle AS, Quesne MG, Sastri CV, Banse F, De Visser SP. Differences and comparisons of the properties and reactivities of iron(III)-hydroperoxo complexes with saturated coordination sphere Chemistry - a European Journal. 21: 1221-1236. DOI: 10.1002/chem.201404918 |
0.677 |
|
| 2015 |
Sahoo D, Quesne MG, De Visser SP, Rath SP. Hydrogen-bonding interactions trigger a spin-flip in iron(III) porphyrin complexes Angewandte Chemie - International Edition. 54: 4796-4800. DOI: 10.1002/anie.201411399 |
0.696 |
|
| 2014 |
Kumar S, Faponle AS, Barman P, Vardhaman AK, Sastri CV, Kumar D, de Visser SP. Long-range electron transfer triggers mechanistic differences between iron(IV)-oxo and iron(IV)-imido oxidants. Journal of the American Chemical Society. 136: 17102-15. PMID 25392052 DOI: 10.1021/Ja508403W |
0.331 |
|
| 2014 |
Jastrzebski R, Quesne MG, Weckhuysen BM, de Visser SP, Bruijnincx PC. Experimental and computational evidence for the mechanism of intradiol catechol dioxygenation by non-heme iron(III) complexes. Chemistry (Weinheim An Der Bergstrasse, Germany). 20: 15686-91. PMID 25322920 DOI: 10.1002/Chem.201404988 |
0.71 |
|
| 2014 |
Neu HM, Quesne MG, Yang T, Prokop-Prigge KA, Lancaster KM, Donohoe J, DeBeer S, de Visser SP, Goldberg DP. Dramatic influence of an anionic donor on the oxygen-atom transfer reactivity of a Mn(V) -oxo complex. Chemistry (Weinheim An Der Bergstrasse, Germany). 20: 14584-8. PMID 25256417 DOI: 10.1002/Chem.201404349 |
0.685 |
|
| 2014 |
Sahu S, Quesne MG, Davies CG, Dürr M, Ivanovi?-Burmazovi? I, Siegler MA, Jameson GN, de Visser SP, Goldberg DP. Direct observation of a nonheme iron(IV)-oxo complex that mediates aromatic C-F hydroxylation. Journal of the American Chemical Society. 136: 13542-5. PMID 25246108 DOI: 10.1021/Ja507346T |
0.702 |
|
| 2014 |
Neu HM, Yang T, Baglia RA, Yosca TH, Green MT, Quesne MG, de Visser SP, Goldberg DP. Oxygen-atom transfer reactivity of axially ligated Mn(V)-oxo complexes: evidence for enhanced electrophilic and nucleophilic pathways. Journal of the American Chemical Society. 136: 13845-52. PMID 25238495 DOI: 10.1021/Ja507177H |
0.672 |
|
| 2014 |
Karamzadeh B, Singh D, Nam W, Kumar D, de Visser SP. Properties and reactivities of nonheme iron(IV)-oxo versus iron(V)-oxo: long-range electron transfer versus hydrogen atom abstraction. Physical Chemistry Chemical Physics : Pccp. 16: 22611-22. PMID 25231726 DOI: 10.1039/C4Cp03053B |
0.315 |
|
| 2014 |
Ji L, Zhang J, Liu W, de Visser SP. Metabolism of halogenated alkanes by cytochrome P450 enzymes. Aerobic oxidation versus anaerobic reduction. Chemistry, An Asian Journal. 9: 1175-82. PMID 24501011 DOI: 10.1002/asia.201301608 |
0.34 |
|
| 2014 |
Hernandez-Ortega A, Quesne MG, Bui S, Heuts DP, Steiner RA, Heyes DJ, de Visser SP, Scrutton NS. Origin of the proton-transfer step in the cofactor-free (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase: effect of the basicity of an active site His residue. The Journal of Biological Chemistry. 289: 8620-32. PMID 24482238 DOI: 10.1074/Jbc.M113.543033 |
0.693 |
|
| 2014 |
Quesne MG, Latifi R, Gonzalez-Ovalle LE, Kumar D, de Visser SP. Quantum mechanics/molecular mechanics study on the oxygen binding and substrate hydroxylation step in AlkB repair enzymes. Chemistry (Weinheim An Der Bergstrasse, Germany). 20: 435-46. PMID 24339041 DOI: 10.1002/Chem.201303282 |
0.695 |
|
| 2014 |
de Visser SP, Quesne MG, Martin B, Comba P, Ryde U. Computational modelling of oxygenation processes in enzymes and biomimetic model complexes. Chemical Communications (Cambridge, England). 50: 262-82. PMID 24256691 DOI: 10.1039/C3Cc47148A |
0.648 |
|
| 2013 |
Quesne MG, Ward RA, de Visser SP. Cysteine protease inhibition by nitrile-based inhibitors: a computational study. Frontiers in Chemistry. 1: 39. PMID 24790966 DOI: 10.3389/Fchem.2013.00039 |
0.682 |
|
| 2013 |
de Visser SP, Porro CS, Quesne MG, Sainna MA, Munro AW. Overview on theoretical studies discriminating the two-oxidant versus two-state-reactivity models for substrate monoxygenation by cytochrome p450 enzymes Current Topics in Medicinal Chemistry. 13: 2218-2232. PMID 24047138 DOI: 10.2174/15680266113136660155 |
0.827 |
|
| 2013 |
Sahu S, Widger LR, Quesne MG, de Visser SP, Matsumura H, Moënne-Loccoz P, Siegler MA, Goldberg DP. Secondary coordination sphere influence on the reactivity of nonheme iron(II) complexes: an experimental and DFT approach. Journal of the American Chemical Society. 135: 10590-3. PMID 23834409 DOI: 10.1021/Ja402688T |
0.692 |
|
| 2013 |
Kumar D, Latifi R, Kumar S, Rybak-Akimova EV, Sainna MA, de Visser SP. Rationalization of the barrier height for p-Z-styrene epoxidation by iron(IV)-oxo porphyrin cation radicals with variable axial ligands. Inorganic Chemistry. 52: 7968-79. PMID 23822112 DOI: 10.1021/Ic4005104 |
0.811 |
|
| 2013 |
Latifi R, Sainna MA, Rybak-Akimova EV, de Visser SP. Does hydrogen-bonding donation to manganese(IV)-oxo and iron(IV)-oxo oxidants affect the oxygen-atom transfer ability? A computational study. Chemistry (Weinheim An Der Bergstrasse, Germany). 19: 4058-68. PMID 23362213 DOI: 10.1002/Chem.201202811 |
0.796 |
|
| 2012 |
Gonzalez-Ovalle LE, Quesne MG, Kumar D, Goldberg DP, de Visser SP. Axial and equatorial ligand effects on biomimetic cysteine dioxygenase model complexes. Organic & Biomolecular Chemistry. 10: 5401-9. PMID 22714822 DOI: 10.1039/C2Ob25406A |
0.678 |
|
| 2012 |
Quesne MG, De Visser SP. Regioselectivity of substrate hydroxylation versus halogenation by a nonheme iron(IV)-oxo complex: Possibility of rearrangement pathways Journal of Biological Inorganic Chemistry. 17: 841-852. PMID 22580819 DOI: 10.1007/S00775-012-0901-4 |
0.734 |
|
| 2012 |
Cho KB, Chen H, Janardanan D, De Visser SP, Shaik S, Nam W. Nonheme iron-oxo and -superoxo reactivities: O 2 binding and spin inversion probability matter Chemical Communications. 48: 2189-2191. PMID 22252386 DOI: 10.1039/C2Cc17610F |
0.791 |
|
| 2012 |
Latifi R, Tahsini L, Nam W, de Visser SP. Regioselectivity of aliphatic versus aromatic hydroxylation by a nonheme iron(II)-superoxo complex. Physical Chemistry Chemical Physics : Pccp. 14: 2518-24. PMID 22252092 DOI: 10.1039/C2Cp23352E |
0.363 |
|
| 2012 |
Kumar D, Sastry GN, de Visser SP. Axial ligand effect on the rate constant of aromatic hydroxylation by iron(IV)-oxo complexes mimicking cytochrome P450 enzymes. The Journal of Physical Chemistry. B. 116: 718-30. PMID 22132821 DOI: 10.1021/Jp2113522 |
0.621 |
|
| 2012 |
Kumar D, Sastry GN, Goldberg DP, de Visser SP. Mechanism of S-oxygenation by a cysteine dioxygenase model complex. The Journal of Physical Chemistry. A. 116: 582-91. PMID 22091701 DOI: 10.1021/Jp208230G |
0.602 |
|
| 2012 |
Kumar D, Sastry GN, De Visser SP. Axial ligand effect on the rate constant of aromatic hydroxylation by iron(IV)-Oxo complexes mimicking cytochrome P450 enzymes Journal of Physical Chemistry B. 116: 718-730. DOI: 10.1021/jp2113522 |
0.55 |
|
| 2011 |
Latifi R, Tahsini L, Kumar D, Sastry GN, Nam W, de Visser SP. Oxidative properties of a nonheme Ni(II)(O2) complex: Reactivity patterns for C-H activation, aromatic hydroxylation and heteroatom oxidation. Chemical Communications (Cambridge, England). 47: 10674-6. PMID 21892444 DOI: 10.1039/C1Cc13993B |
0.528 |
|
| 2011 |
Prokop KA, Neu HM, de Visser SP, Goldberg DP. A manganese(V)-oxo π-cation radical complex: influence of one-electron oxidation on oxygen-atom transfer. Journal of the American Chemical Society. 133: 15874-7. PMID 21888343 DOI: 10.1021/Ja2066237 |
0.306 |
|
| 2011 |
Kumar D, Sastry GN, De Visser SP. Effect of the axial ligand on substrate sulfoxidation mediated by iron(IV)-oxo porphyrin cation radical oxidants Chemistry - a European Journal. 17: 6196-6205. PMID 21469227 DOI: 10.1002/Chem.201003187 |
0.612 |
|
| 2011 |
Kumar D, Thiel W, De Visser SP. Theoretical study on the mechanism of the oxygen activation process in cysteine dioxygenase enzymes Journal of the American Chemical Society. 133: 3869-3882. PMID 21344861 DOI: 10.1021/Ja107514F |
0.36 |
|
| 2011 |
de Visser SP, Latifi R, Tahsini L, Nam W. The axial ligand effect on aliphatic and aromatic hydroxylation by non-heme iron(IV)-oxo biomimetic complexes. Chemistry, An Asian Journal. 6: 493-504. PMID 21254427 DOI: 10.1002/Asia.201000586 |
0.334 |
|
| 2011 |
Latifi R, Tahsini L, Karamzadeh B, Safari N, Nam W, de Visser SP. Manganese substituted Compound I of cytochrome P450 biomimetics: a comparative reactivity study of Mn(V)-oxo versus Mn(IV)-oxo species. Archives of Biochemistry and Biophysics. 507: 4-13. PMID 21216220 DOI: 10.1016/J.Abb.2010.12.035 |
0.38 |
|
| 2010 |
Karamzadeh B, Kumar D, Sastry GN, De Visser SP. Steric factors override thermodynamic driving force in regioselectivity of proline hydroxylation by prolyl-4-hydroxylase enzymes Journal of Physical Chemistry A. 114: 13234-13243. PMID 21114303 DOI: 10.1021/Jp1089855 |
0.535 |
|
| 2010 |
Kumar D, Karamzadeh B, Sastry GN, De Visser SP. What factors influence the rate constant of substrate epoxidation by compound i of cytochrome P450 and analogous iron(IV)-oxo oxidants? Journal of the American Chemical Society. 132: 7656-7667. PMID 20481499 DOI: 10.1021/Ja9106176 |
0.62 |
|
| 2010 |
De Visser SP. Trends in substrate hydroxylation reactions by heme and nonheme iron(IV)-oxo oxidants give correlations between intrinsic properties of the oxidant with barrier height Journal of the American Chemical Society. 132: 1087-1097. PMID 20041691 DOI: 10.1021/ja908340j |
0.388 |
|
| 2009 |
Porro CS, Kumar D, De Visser SP. Electronic properties of pentacoordinated heme complexes in cytochrome P450 enzymes: Search for an Fe(i) oxidation state Physical Chemistry Chemical Physics. 11: 10219-10226. PMID 19865780 DOI: 10.1039/b911966c |
0.366 |
|
| 2009 |
Kumar D, Tahsini L, De Visser SP, Kang HY, Kim SJ, Nam W. Effect of porphyrin ligands on the regioselective dehydrogenation versus epoxidation of olefins by oxoiron(IV) mimics of cytochrome P450 Journal of Physical Chemistry A. 113: 11713-11722. PMID 19658379 DOI: 10.1021/Jp9028694 |
0.374 |
|
| 2009 |
Porro CS, Sutcliffe MJ, De Visser SP. Quantum mechanics/molecular mechanics studies on the sulfoxidation of dimethyl sulfide by compound i and compound 0 of cytochrome p450: Which is the better oxidant Journal of Physical Chemistry A. 113: 11635-11642. PMID 19534515 DOI: 10.1021/jp9023926 |
0.318 |
|
| 2009 |
Latifi R, Bagherzadeh M, de Visser SP. Origin of the correlation of the rate constant of substrate hydroxylation by nonheme iron(IV)-oxo complexes with the bond-dissociation energy of the C-H bond of the substrate. Chemistry (Weinheim An Der Bergstrasse, Germany). 15: 6651-62. PMID 19472231 DOI: 10.1002/Chem.200900211 |
0.38 |
|
| 2009 |
Tahsini L, Bagherzadeh M, Nam W, De Visser SP. Fundamental differences of substrate hydroxylation by high-valent Lron(IV)-Oxo models of cytochrome P450 Inorganic Chemistry. 48: 6661-6669. PMID 19469505 DOI: 10.1021/Ic900593C |
0.322 |
|
| 2009 |
De Visser SP, Tahsini L, Nam W. How does the axial ligand of cytochrome p450 biomimetics influence the regioselectivity of aliphatic versus aromatic hydroxylation? Chemistry - a European Journal. 15: 5577-5587. PMID 19347895 DOI: 10.1002/Chem.200802234 |
0.362 |
|
| 2009 |
de Visser SP. Density functional theory (DFT) and combined quantum mechanical/molecular mechanics (QM/MM) studies on the oxygen activation step in nitric oxide synthase enzymes Biochemical Society Transactions. 37: 373-377. PMID 19290865 DOI: 10.1042/BST0370373 |
0.309 |
|
| 2009 |
De Visser SP, Straganz GD. Why do cysteine dioxygenase enzymes contain a 3-his ligand motif rather than a 2His/lAsp motif like most nonheme dioxygenases? Journal of Physical Chemistry A. 113: 1835-1846. PMID 19199799 DOI: 10.1021/jp809700f |
0.365 |
|
| 2009 |
de Visser SP, Latifi R. Carbon dioxide: a waste product in the catalytic cycle of alpha-ketoglutarate dependent halogenases prevents the formation of hydroxylated by-products. The Journal of Physical Chemistry. B. 113: 12-4. PMID 19061416 DOI: 10.1021/Jp8097632 |
0.345 |
|
| 2008 |
de Visser SP, Derat E, Kumar D. A tribute to Sason Shaik. The Journal of Physical Chemistry. A. 112: 12721-3. PMID 19072248 DOI: 10.1021/Jp8063454 |
0.512 |
|
| 2008 |
De Visser SP, Lee ST. Is the bound substrate in nitric oxide synthase protonated or neutral and what is the active oxidant that performs substrate hydroxylation? Journal of the American Chemical Society. 130: 12961-12974. PMID 18774806 DOI: 10.1021/ja8010995 |
0.369 |
|
| 2008 |
Shaik S, Kumar D, de Visser SP. A valence bond modeling of trends in hydrogen abstraction barriers and transition states of hydroxylation reactions catalyzed by cytochrome P450 enzymes. Journal of the American Chemical Society. 130: 10128-40. PMID 18616242 DOI: 10.1021/Ja8019615 |
0.568 |
|
| 2008 |
Balding PR, Porro CS, McLean KJ, Sutcliffe MJ, Maréchal JD, Munro AW, De Visser SP. How do azoles inhibit cytochrome P450 enzymes? A density functional study Journal of Physical Chemistry A. 112: 12911-12918. PMID 18563875 DOI: 10.1021/jp802087w |
0.32 |
|
| 2008 |
de Visser SP. Is the mu-oxo-mu-peroxodiiron intermediate of a ribonucleotide reductase biomimetic a possible oxidant of epoxidation reactions? Chemistry (Weinheim An Der Bergstrasse, Germany). 14: 4533-4541. PMID 18386299 DOI: 10.1002/chem.200701802 |
0.363 |
|
| 2008 |
Godfrey E, Porro CS, de Visser SP. Comparative quantum mechanics/molecular mechanics (QM/MM) and density functional theory calculations on the oxo-iron species of taurine/alpha-ketoglutarate dioxygenase. The Journal of Physical Chemistry. A. 112: 2464-8. PMID 18237159 DOI: 10.1021/jp710999v |
0.337 |
|
| 2008 |
Shaik S, Kumar D, De Visser SP. A valence bond modeling of trends in hydrogen abstraction barriers and transition states of hydroxylation reactions catalyzed by cytochrome P450 enzymes (Journal of the American Chemical Society (2008) 130, (10128-10140)) Journal of the American Chemical Society. 130: 14016. DOI: 10.1021/Ja806917F |
0.484 |
|
| 2008 |
De Visser SP, Lee YM, Nam W. Theoretical investigation on the mechanism of oxygen atom transfer between two non-heme iron centres European Journal of Inorganic Chemistry. 1027-1030. DOI: 10.1002/Ejic.200800014 |
0.325 |
|
| 2007 |
Aluri S, De Visser SP. The mechanism of cysteine oxygenation by cysteine dioxygenase enzymes Journal of the American Chemical Society. 129: 14846-14847. PMID 17994747 DOI: 10.1021/ja0758178 |
0.378 |
|
| 2007 |
Wang R, de Visser SP. How does the push/pull effect of the axial ligand influence the catalytic properties of Compound I of catalase and cytochrome P450? Journal of Inorganic Biochemistry. 101: 1464-1472. PMID 17659781 DOI: 10.1016/j.jinorgbio.2007.06.022 |
0.361 |
|
| 2007 |
De Visser SP, Oh K, Han AR, Nam W. Combined experimental and theoretical study on aromatic hydroxylation by mononuclear nonheme iron(IV)-oxo complexes Inorganic Chemistry. 46: 4632-4641. PMID 17444641 DOI: 10.1021/Ic700462H |
0.36 |
|
| 2007 |
Hazan C, Kumar D, De Visser SP, Shaik S. A density functional study of the factors that influence the regioselectivity of toluene hydroxylation by cytochrome P450 enzymes European Journal of Inorganic Chemistry. 2966-2974. DOI: 10.1002/Ejic.200700117 |
0.746 |
|
| 2006 |
De Visser SP. What factors influence the ratio of C-H hydroxylation versus C=C epoxidation by a nonheme cytochrome P450 biomimetic? Journal of the American Chemical Society. 128: 15809-15818. PMID 17147391 DOI: 10.1021/ja065365j |
0.399 |
|
| 2006 |
De Visser SP. What external perturbations influence the electronic properties of catalase compound I? Inorganic Chemistry. 45: 9551-9557. PMID 17083257 DOI: 10.1021/ic061019r |
0.319 |
|
| 2006 |
De Visser SP. Substitution of hydrogen by deuterium changes the regioselectivity of ethylbenzene hydroxylation by an oxo-iron-porphyrin catalyst Chemistry - a European Journal. 12: 8168-8177. PMID 16871510 DOI: 10.1002/chem.200600376 |
0.38 |
|
| 2006 |
De Visser SP. Propene activation by the oxo-iron active species of taurine/α- ketoglutarate dioxygenase (TauD) enzyme. How does the catalysis compare to heme-enzymes? Journal of the American Chemical Society. 128: 9813-9824. PMID 16866538 DOI: 10.1021/ja061581g |
0.409 |
|
| 2006 |
De Visser SP, Kumar D, Danovich M, Nevo N, Danovich D, Sharma PK, Wu W, Shaik S. Ferromagnetic bonding: High spin copper clusters (n+1Cu n; n = 2-14) devoid of electron pairs but possessing strong bonding Journal of Physical Chemistry A. 110: 8510-8518. PMID 16821835 DOI: 10.1021/Jp055125A |
0.596 |
|
| 2006 |
De Visser SP. The axial ligand effect of oxo-iron porphyrin catalysts. How does chloride compare to thiolate? Journal of Biological Inorganic Chemistry. 11: 168-178. PMID 16331402 DOI: 10.1007/s00775-005-0061-x |
0.325 |
|
| 2005 |
Kumar D, Hirao H, De Visser SP, Zheng J, Wang D, Thiel W, Shaik S. New features in the catalytic cycle of cytochrome P450 during the formation of Compound I from Compound 0 Journal of Physical Chemistry B. 109: 19946-19951. PMID 16853579 DOI: 10.1021/Jp054754H |
0.5 |
|
| 2005 |
De Visser SP. What affects the quartet - Doublet energy splitting in peroxidase enzymes? Journal of Physical Chemistry A. 109: 11050-11057. PMID 16331950 DOI: 10.1021/jp053873u |
0.3 |
|
| 2005 |
Shaik S, Kumar D, de Visser SP, Altun A, Thiel W. Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes. Chemical Reviews. 105: 2279-328. PMID 15941215 DOI: 10.1021/Cr030722J |
0.428 |
|
| 2005 |
Kumar D, De Visser SP, Shaik S. Theory favors a stepwise mechanism of porphyrin degradation by a ferric hydroperoxide model of the active species of heme oxygenase Journal of the American Chemical Society. 127: 8204-8213. PMID 15926850 DOI: 10.1021/Ja0446956 |
0.473 |
|
| 2005 |
Kumar D, de Visser SP, Sharma PK, Hirao H, Shaik S. Sulfoxidation mechanisms catalyzed by cytochrome P450 and horseradish peroxidase models: spin selection induced by the ligand. Biochemistry. 44: 8148-58. PMID 15924434 DOI: 10.1021/Bi050348C |
0.672 |
|
| 2005 |
Kumar D, de Visser SP, Shaik S. Multistate reactivity in styrene epoxidation by compound I of cytochrome p450: mechanisms of products and side products formation. Chemistry (Weinheim An Der Bergstrasse, Germany). 11: 2825-35. PMID 15744771 DOI: 10.1002/Chem.200401044 |
0.517 |
|
| 2005 |
Kumar D, de Visser SP, Sharma PK, Derat E, Shaik S. The intrinsic axial ligand effect on propene oxidation by horseradish peroxidase versus cytochrome P450 enzymes. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 181-9. PMID 15723206 DOI: 10.1007/S00775-004-0622-4 |
0.778 |
|
| 2005 |
Shaik S, De Visser SP. Computational approaches to cytochrome P450 function Cytochrome P450: Structure, Mechanism, and Biochemistry: Third Edition. 45-85. DOI: 10.1007/0-387-27447-2_2 |
0.379 |
|
| 2004 |
de Visser SP, Kumar D, Neumann R, Shaik S. Computer-generated high-valent iron--oxo and manganese--oxo species with polyoxometalate ligands: how do they compare with the iron--oxo active species of heme enzymes? Angewandte Chemie (International Ed. in English). 43: 5661-5. PMID 15495193 DOI: 10.1002/Anie.200453867 |
0.449 |
|
| 2004 |
Shaik S, de Visser SP, Kumar D. External electric field will control the selectivity of enzymatic-like bond activations. Journal of the American Chemical Society. 126: 11746-9. PMID 15366922 DOI: 10.1021/Ja047432K |
0.405 |
|
| 2004 |
Shaik S, de Visser SP, Kumar D. One oxidant, many pathways: a theoretical perspective of monooxygenation mechanisms by cytochrome P450 enzymes. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 661-8. PMID 15365903 DOI: 10.1007/S00775-004-0576-6 |
0.496 |
|
| 2004 |
Meunier B, de Visser SP, Shaik S. Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes. Chemical Reviews. 104: 3947-80. PMID 15352783 DOI: 10.1021/Cr020443G |
0.478 |
|
| 2004 |
de Visser SP, Kumar D, Cohen S, Shacham R, Shaik S. A predictive pattern of computed barriers for C-h hydroxylation by compound I of cytochrome p450. Journal of the American Chemical Society. 126: 8362-3. PMID 15237977 DOI: 10.1021/Ja048528H |
0.525 |
|
| 2004 |
de Visser SP, Kumar D, Shaik S. How do aldehyde side products occur during alkene epoxidation by cytochrome P450? Theory reveals a state-specific multi-state scenario where the high-spin component leads to all side products. Journal of Inorganic Biochemistry. 98: 1183-93. PMID 15219984 DOI: 10.1016/J.Jinorgbio.2004.01.015 |
0.516 |
|
| 2004 |
Kumar D, De Visser SP, Shaik S. Oxygen Economy of Cytochrome P450: What is the Origin of the Mixed Functionality as a Dehydrogenase-Oxidase Enzyme Compared with its Normal Function? Journal of the American Chemical Society. 126: 5072-5073. PMID 15099082 DOI: 10.1021/Ja0318737 |
0.462 |
|
| 2004 |
Groenhof G, Bouxin-Cademartory M, Hess B, De Visser SP, Berendsen HJ, Olivucci M, Mark AE, Robb MA. Photoactivation of the photoactive yellow protein: why photon absorption triggers a trans-to-cis Isomerization of the chromophore in the protein. Journal of the American Chemical Society. 126: 4228-33. PMID 15053611 DOI: 10.1021/Ja039557F |
0.663 |
|
| 2004 |
Sharma PK, Kevorkiants R, de Visser SP, Kumar D, Shaik S. Porphyrin traps its terminator! Concerted and stepwise porphyrin degradation mechanisms induced by heme-oxygenase and cytochrome p450. Angewandte Chemie (International Ed. in English). 43: 1129-32. PMID 14983454 DOI: 10.1002/Anie.200352943 |
0.597 |
|
| 2004 |
Kumar D, de Visser SP, Sharma PK, Cohen S, Shaik S. Radical clock substrates, their C-H hydroxylation mechanism by cytochrome P450, and other reactivity patterns: what does theory reveal about the clocks' behavior? Journal of the American Chemical Society. 126: 1907-20. PMID 14871124 DOI: 10.1021/Ja039439S |
0.688 |
|
| 2004 |
Shaik S, Cohen S, De Visser SP, Sharma PK, Kumar D, Kozuch S, Ogliaro F, Danovich D. The "Rebound Controversy": An Overview and Theoretical Modeling of the Rebound Step in C-H Hydroxylation by Cytochrome P450 European Journal of Inorganic Chemistry. 207-226. |
0.782 |
|
| 2003 |
de Visser SP, Shaik S, Sharma PK, Kumar D, Thiel W. Active species of horseradish peroxidase (HRP) and cytochrome P450: two electronic chameleons. Journal of the American Chemical Society. 125: 15779-88. PMID 14677968 DOI: 10.1021/Ja0380906 |
0.611 |
|
| 2003 |
Kumar D, De Visser SP, Shaik S. How Does Product Isotope Effect Prove the Operation of a Two-State "Rebound" Mechanism in C-H Hydroxylation by Cytochrome P450? Journal of the American Chemical Society. 125: 13024-13025. PMID 14570465 DOI: 10.1021/Ja036906X |
0.534 |
|
| 2003 |
Ben-Daniel R, de Visser SP, Shaik S, Neumann R. Electrophilic aromatic chlorination and haloperoxidation of chloride catalyzed by polyfluorinated alcohols: a new manifestation of template catalysis. Journal of the American Chemical Society. 125: 12116-7. PMID 14518997 DOI: 10.1021/Ja0364524 |
0.396 |
|
| 2003 |
Sharma PK, De Visser SP, Shaik S. Can a single oxidant with two spin states masquerade as two different oxidants? A study of the sulfoxidation mechanism by cytochrome p450. Journal of the American Chemical Society. 125: 8698-9. PMID 12862444 DOI: 10.1021/Ja035135U |
0.649 |
|
| 2003 |
de Visser SP, Shaik S. A proton-shuttle mechanism mediated by the porphyrin in benzene hydroxylation by cytochrome p450 enzymes. Journal of the American Chemical Society. 125: 7413-24. PMID 12797816 DOI: 10.1021/Ja034142F |
0.564 |
|
| 2003 |
de Visser SP, Kaneti J, Neumann R, Shaik S. Fluorinated alcohols enable olefin epoxidation by H2O2: template catalysis. The Journal of Organic Chemistry. 68: 2903-12. PMID 12662068 DOI: 10.1021/Jo034087T |
0.395 |
|
| 2003 |
Sharma PK, De Visser SP, Ogliaro F, Shaik S. Is the ruthenium analogue of compound I of cytochrome P450 an efficient oxidant? A theoretical investigation of the methane hydroxylation reaction Journal of the American Chemical Society. 125: 2291-2300. PMID 12590559 DOI: 10.1021/Ja0282487 |
0.809 |
|
| 2003 |
De Visser SP, Danovich D, Shaik S. Ferromagnetic bonding in high-spin alkali-metal clusters. How does sodium compare to lithium? Physical Chemistry Chemical Physics. 5: 158-164. DOI: 10.1039/B207155J |
0.398 |
|
| 2003 |
De Visser SP, Kaneti J, Neumann R, Shaik S. Fluorinated alcohols enable olefin epoxidation by H2O2: Template catalysis Journal of Organic Chemistry. 68: 2903-2912. DOI: 10.1021/jo034087t |
0.326 |
|
| 2003 |
Ben-Daniel R, De Visser SP, Shaik S, Neumann R. Electrophilic aromatic chlorination and haloperoxidation of chloride catalyzed by polyfluorinated alcohols: A new manifestation of template catalysis Journal of the American Chemical Society. 125: 12116-12117. DOI: 10.1021/ja0364524 |
0.331 |
|
| 2002 |
De Visser SP, Ogliaro F, Sharma PK, Shaik S. Hydrogen bonding modulates the selectivity of enzymatic oxidation by P450: Chameleon oxidant behavior by compound I Angewandte Chemie - International Edition. 41: 1947-1951. PMID 19750642 DOI: 10.1002/1521-3773(20020603)41:11<1947::Aid-Anie1947>3.0.Co;2-W |
0.752 |
|
| 2002 |
Shaik S, De Visser SP, Ogliaro F, Schwarz H, Schröder D. Two-state reactivity mechanisms of hydroxylation and epoxidation by cytochrome P-450 revealed by theory Current Opinion in Chemical Biology. 6: 556-567. PMID 12413538 DOI: 10.1016/S1367-5931(02)00363-0 |
0.745 |
|
| 2002 |
De Visser SP, Ogliaro F, Sharma PK, Shaik S. What factors affect the regioselectivity of oxidation by cytochrome P450? A DFT study of allylic hydroxylation and double bond epoxidation in a model reaction Journal of the American Chemical Society. 124: 11809-11826. PMID 12296749 DOI: 10.1021/Ja026872D |
0.784 |
|
| 2002 |
Ogliaro F, De Visser SP, Shaik S. The 'push' effect of the thiolate ligand in cytochrome P450: A theoretical gauging Journal of Inorganic Biochemistry. 91: 554-567. PMID 12237222 DOI: 10.1016/S0162-0134(02)00437-3 |
0.735 |
|
| 2002 |
Ogliaro F, De Visser SP, Cohen S, Sharma PK, Shaik S. Searching for the second oxidant in the catalytic cycle of cytochrome P450: A theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways Journal of the American Chemical Society. 124: 2806-2817. PMID 11890833 DOI: 10.1021/Ja0171963 |
0.809 |
|
| 2002 |
Shaik S, De Visser SP, Wu W, Song L, Hiberty PC. Reply to comment on "identity hydrogen abstraction reactions, X• + H-X′ → X-H + X′• (X = X′ = CH3, SiH3, GeH3, SnH3, PbH3): A valence bond modeling" Journal of Physical Chemistry A. 106: 5043-5045. DOI: 10.1021/Jp015589I |
0.434 |
|
| 2002 |
De Visser SP, Danovich D, Wu W, Shaik S. Ferromagnetic bonding: Properties of high-spin lithium clusters n+1Lin (n = 2-12) devoid of electron pairs Journal of Physical Chemistry A. 106: 4961-4969. DOI: 10.1021/Jp014665E |
0.468 |
|
| 2001 |
Ogliaro F, de Visser SP, Groves JT, Shaik S. Chameleon States: High-Valent Metal-Oxo Species of Cytochrome P450 and Its Ruthenium Analogue. Angewandte Chemie (International Ed. in English). 40: 2874-2878. PMID 29711990 DOI: 10.1002/1521-3773(20010803)40:15<2874::Aid-Anie2874>3.0.Co;2-9 |
0.493 |
|
| 2001 |
de Visser SP, Ogliaro F, Shaik S. How Does Ethene Inactivate Cytochrome P450 En Route to Its Epoxidation? A Density Functional Study. Angewandte Chemie (International Ed. in English). 40: 2871-2874. PMID 29711977 DOI: 10.1002/1521-3773(20010803)40:15<2871::Aid-Anie2871>3.0.Co;2-R |
0.463 |
|
| 2001 |
de Visser SP, Ogliaro F, Shaik S. Stereospecific oxidation by compound I of cytochrome P450 does not proceed in a concerted synchronous manner. Chemical Communications (Cambridge, England). 2322-3. PMID 12240056 DOI: 10.1039/B105571M |
0.706 |
|
| 2001 |
Ogliaro F, de Visser SP, Cohen S, Kaneti J, Shaik S. The experimentally elusive oxidant of cytochrome P450: a theoretical "trapping" defining more closely the "real" species. Chembiochem : a European Journal of Chemical Biology. 2: 848-51. PMID 11948872 DOI: 10.1002/1439-7633(20011105)2:11<848::Aid-Cbic848>3.0.Co;2-0 |
0.706 |
|
| 2001 |
De Visser SP, Ogliaro F, Gross Z, Shaik S. What is the difference between the manganese porphyrin and corrole analogues of cytochrome P450's compound I? Chemistry - a European Journal. 7: 4954-4960. PMID 11763464 DOI: 10.1002/1521-3765(20011119)7:22<4954::Aid-Chem4954>3.0.Co;2-U |
0.721 |
|
| 2001 |
Ogliaro F, de Visser SP, Groves JT, Shaik S. Chameleon States: High-Valent Metal-Oxo Species of Cytochrome P450 and Its Ruthenium Analogue The research in HU was sponsored by the Binational German Israeli Foundation (GIF) and by the Israeli Ministry of Science, Culture and Sport. Partial support by the US National Science Foundation (CHE-9814301) to J.T.G. is acknowledged. F.O. thanks the EU for a Marie Curie Fellowship. Angewandte Chemie (International Ed. in English). 40: 3503. PMID 11592182 DOI: 10.1002/1521-3773(20011001)40:19<3503::Aid-Anie33333503>3.0.Co;2-O |
0.694 |
|
| 2001 |
Ogliaro F, de Visser SP, Groves JT, Shaik S. Chameleon States: High-Valent Metal-Oxo Species of Cytochrome P450 and Its Ruthenium Analogue The research in HU was sponsored by the Binational German Israeli Foundation (GIF) and by the Israeli Ministry of Science, Culture and Sport. Partial support by the US National Science Foundation (CHE-9814301) to J.T.G. is acknowledged. F.O. thanks the EU for a Marie Curie Fellowship. Angewandte Chemie (International Ed. in English). 40: 2874-2878. PMID 11500894 DOI: 10.1002/1521-3773(20010803)40:15<2874::AID-ANIE2874>3.0.CO;2-9 |
0.694 |
|
| 2001 |
de Visser SP, Ogliaro F, Shaik S. How Does Ethene Inactivate Cytochrome P450 En Route to Its Epoxidation? A Density Functional Study The research is supported in part by the ISF and in part by the Ministry of Science, Culture, and Sport. F.O. acknowledges the European Union for a Marie Curie Fellowship. Angewandte Chemie (International Ed. in English). 40: 2871-2874. PMID 11500893 DOI: 10.1002/1521-3773(20010803)40:15<2871::AID-ANIE2871>3.0.CO;2-R |
0.683 |
|
| 2001 |
De Visser SP, Ogliaro F, Harris N, Shaik S. Multi-state epoxidation of ethene by cytochrome P450: A quantum chemical study Journal of the American Chemical Society. 123: 3037-3047. PMID 11457014 DOI: 10.1021/Ja003544+ |
0.757 |
|
| 2001 |
De Visser SP, Filatov M, Shaik S. Myers-Saito and Schmittel cyclization of hepta-1,2,4-triene-6-yne: A theoretical REKS study Physical Chemistry Chemical Physics. 3: 1242-1245. DOI: 10.1039/B009965L |
0.58 |
|
| 2001 |
Ogliaro F, De Visser SP, Groves JT, Shaik S. Chameleon states: High-valent metal-oxo species of cytochrome P450 and its ruthenium analogue Angewandte Chemie - International Edition. 40: 2874-2878. DOI: 10.1002/1521-3773(20010803)40:15<2874::AID-ANIE2874>3.0.CO;2-9 |
0.71 |
|
| 2001 |
De Visser SP, Ogliaro F, Shaik S. How does ethene inactivate cytochrome P450 en route to its epoxidation? A density functional study Angewandte Chemie - International Edition. 40: 2871-2874. DOI: 10.1002/1521-3773(20010803)40:15<2871::AID-ANIE2871>3.0.CO;2-R |
0.693 |
|
| 2001 |
De Visser SP, Ogliaro F, Shaik S. Stereospecific oxidation by Compound I of Cytochrome P450 does not proceed in a concerted synchronous manner Chemical Communications. 2322-2323. |
0.666 |
|
| 2000 |
De Visser SP, Filatov M, Shaik S. REKS calculations on ortho-, meta- and para-benzyne Physical Chemistry Chemical Physics. 2: 5046-5048. DOI: 10.1039/B006786P |
0.576 |
|
| 2000 |
Ogliaro F, Harris N, Cohen S, Filatov M, De Visser SP, Shaik S. A model 'rebound' mechanism of hydroxylation by cytochrome P450: Stepwise and effectively concerted pathways, and their reactivity patterns Journal of the American Chemical Society. 122: 8977-8989. DOI: 10.1021/Ja991878X |
0.795 |
|
| 2000 |
Ogliaro F, Cohen S, De Visser SP, Shaik S. Medium polarization and hydrogen bonding effects on compound I of cytochrome P450: What kind of a radical is it really? [15] Journal of the American Chemical Society. 122: 12892-12893. DOI: 10.1021/Ja005619F |
0.731 |
|
| 1998 |
De Visser SP, Bickelhaupt FM, De Koning LJ, Nibbering NMM. Sulfur-sulfur three-electron bond dissociation enthalpies of dialkyl sulfide dimer radical cations International Journal of Mass Spectrometry. 179: 43-54. DOI: 10.1016/S1387-3806(98)14072-1 |
0.405 |
|
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