Year |
Citation |
Score |
2011 |
Lai W, Chen H, Cohen S, Shaik S. Will P450 cam hydroxylate or desaturate alkanes? QM and QM/MM studies Journal of Physical Chemistry Letters. 2: 2229-2235. DOI: 10.1021/Jz2007534 |
0.631 |
|
2010 |
Shaik S, Cohen S, Wang Y, Chen H, Kumar D, Thiel W. P450 enzymes: their structure, reactivity, and selectivity-modeled by QM/MM calculations. Chemical Reviews. 110: 949-1017. PMID 19813749 DOI: 10.1021/Cr900121S |
0.531 |
|
2009 |
Jiang Y, Sivaramakrishnan S, Hayashi T, Cohen S, Moënne-Loccoz P, Shaik S, Ortiz de Montellano PR. Calculated and experimental spin state of seleno cytochrome P450. Angewandte Chemie (International Ed. in English). 48: 7193-5. PMID 19718734 DOI: 10.1002/Anie.200901485 |
0.501 |
|
2008 |
Cho KB, Hirao H, Chen H, Carvajal MA, Cohen S, Derat E, Thiel W, Shaik S. Compound I in heme thiolate enzymes: a comparative QM/MM study. The Journal of Physical Chemistry. A. 112: 13128-38. PMID 18850694 DOI: 10.1021/Jp806770Y |
0.699 |
|
2006 |
Cohen S, Kozuch S, Hazan C, Shaik S. Does substrate oxidation determine the regioselectivity of cyclohexene and propene oxidation by cytochrome p450? Journal of the American Chemical Society. 128: 11028-9. PMID 16925412 DOI: 10.1021/Ja063269C |
0.743 |
|
2006 |
Cohen S, Kumar D, Shaik S. In silico design of a mutant of cytochrome P450 containing selenocysteine. Journal of the American Chemical Society. 128: 2649-53. PMID 16492051 DOI: 10.1021/Ja056586C |
0.483 |
|
2005 |
Derat E, Cohen S, Shaik S, Altun A, Thiel W. Principal active species of horseradish peroxidase, compound I: a hybrid quantum mechanical/molecular mechanical study. Journal of the American Chemical Society. 127: 13611-21. PMID 16190726 DOI: 10.1021/Ja0534046 |
0.67 |
|
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 |
0.616 |
|
2004 |
Schöneboom JC, Cohen S, Lin H, Shaik S, Thiel W. Quantum mechanical/molecular mechanical investigation of the mechanism of C-H hydroxylation of camphor by cytochrome P450cam: theory supports a two-state rebound mechanism. Journal of the American Chemical Society. 126: 4017-34. PMID 15038756 DOI: 10.1021/Ja039847W |
0.513 |
|
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 |
0.711 |
|
2004 |
Lin H, Schöneboom JC, Cohen S, Shaik S, Thiel W. QM/MM Study of the Product−Enzyme Complex in P450camCatalysis The Journal of Physical Chemistry B. 108: 10083-10088. DOI: 10.1021/Jp0493632 |
0.447 |
|
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 Cheminform. 35. DOI: 10.1002/Ejic.200300448 |
0.751 |
|
2004 |
Shaik S, Cohen S, de Visser S, Sharma P, 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. 2004: 207-226. DOI: 10.1002/ejic.200300448 |
0.75 |
|
2002 |
Schöneboom JC, Lin H, Reuter N, Thiel W, Cohen S, Ogliaro F, Shaik S. The elusive oxidant species of cytochrome P450 enzymes: Characterization by combined quantum mechanical/molecular mechanical (QM/MM) calculations Journal of the American Chemical Society. 124: 8142-8151. PMID 12095360 DOI: 10.1021/Ja026279W |
0.744 |
|
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 |
0.757 |
|
2000 |
Ogliaro F, Cohen S, Filatov M, Harris N, Shaik S. The High-Valent Compound of Cytochrome P450: The Nature of the Fe-S Bond and the Role of the Thiolate Ligand as an Internal Electron Donor. Angewandte Chemie (International Ed. in English). 39: 3851-3855. PMID 29711670 DOI: 10.1002/1521-3773(20001103)39:21<3851::Aid-Anie3851>3.0.Co;2-9 |
0.625 |
|
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 |
0.752 |
|
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 |
0.734 |
|
2000 |
Ogliaro F, Cohen S, Filatov M, Harris N, Shaik S. The high-valent compound of cytochrome P450: The nature of the Fe-S bond and the role of the thiolate ligand as an internal electron donor Angewandte Chemie - International Edition. 39: 3851-3855. DOI: 10.1002/1521-3773(20001103)39:21<3851::AID-ANIE3851>3.0.CO;2-9 |
0.704 |
|
2000 |
Harris N, Cohen S, Filatov M, Ogliaro F, Shaik S. Zwei Reaktionswege beim „Wiederanbindungs”-Mechanismus der Alkanhydroxylierung durch Cytochrom P450: Entstehung freier Radikale mit begrenzter Lebensdauer Angewandte Chemie. 112: 2070-2074. DOI: 10.1002/1521-3757(20000602)112:11<2070::Aid-Ange2070>3.0.Co;2-U |
0.73 |
|
Show low-probability matches. |