460
M. G. Quesne and S. P. de Visser
67. Gelb MH, Heimbrook DC, Malkonen P, Sligar SG (1982) Stereochemistry and deuterium isotope effects in camphor hydroxylation by the cytochrome P450cam monooxygenase system.
Biochemistry 21:370–377
68. Davydov DR, Hui Bon Hoa G, Peterson JA (1999) Dynamics of protein-bound water in the
heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam
and P450 2B4. Biochemistry 38:751–761
69. Ruettinger RT, Wen L-P, Fulco AJ (1989) Coding nucleotide, 5’regulatory, and deduced amino
acid sequences of P-450BM-3, a single peptide cytochrome P-450: NADPH-P-450 reductase
from Bacillus megaterium. J Biol Chem 264:10987–10995
70. Grogan G (2011) Cytochromes P450: exploiting diversity and enabling application as biocatalysts. Curr Opin Chem Biol 15:241–248
71. O’Reilly E, Köhler V, Flitsch SL, Turner NJ (2011) Cytochromes P450 as useful biocatalysts:
addressing the limitations. Chem Commun 47:2490–2501
72. Omura T, Sato R (1962) A new cytochrome in liver microsomes. J Biol Chem 237:PC1375PC1376
73. Auclair K, Moënne-Loccoz P, de Montellano PR (2001) Roles of the proximal heme thiolate
ligand in cytochrome P450cam. J Am Chem Soc 123:4877–4885
74. Poulos TL, Finzel BC, Gunsalus IC et al (1985) The 2.6-A crystal structure of Pseudomonas
putida cytochrome P-450. J Biol Chem 260:16122–16130
75. Schlichting I, Berendzen J, Chu K et al (2000) The catalytic pathway of cytochrome P450cam
at atomic resolution. Science (80-) 287:1615–1622
76. Rittle J, Green MT (2010) Cytochrome P450 compound I: capture, characterization, and CH
bond activation kinetics. Science (80-) 330:933–937
77. de Visser SP, Shaik S, Sharma PK et al (2003) Active species of horseradish peroxidase (HRP)
and cytochrome P450: two electronic chameleons. J Am Chem Soc 125:15779–15788. https://
doi.org/10.1021/ja0380906
78. Shaik S, Kumar D, de Visser SP et al (2005) Theoretical perspective on the structure and
mechanism of cytochrome P450 enzymes. Chem Rev 105:2279–2328. https://doi.org/10.
1021/cr030722j
79. Kamachi T, Yoshizawa K (2003) A theoretical study on the mechanism of camphor hydroxylation by compound I of cytochrome P450. J Am Chem Soc 125:4652–4661
80. de Visser SP, Ogliaro F, Shaik S (2001) 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 Cu. Angew Chem Int Ed Engl 40:2871–2874. DOI: https://doi.org/10.1002/15213773(20010803)40:15<2871::AID-ANIE2871>3.0.CO;2-R [pii]
81. Kumar D, de Visser SP, Sharma PK et al (2004) Radical clock substrates, their C-H hydroxylation mechanism by cytochrome P450, and other reactivity patterns: what does theory
reveal about the clocks’ behavior? J Am Chem Soc 126:1907–1920. https://doi.org/10.1021/
ja039439s
82. Quesne MG, Senthilnathan D, Singh D et al (2016) Origin of the enhanced reactivity of μnitrido-bridged diiron(IV)-Oxo porphyrinoid complexes over cytochrome P450 compound i.
ACS Catal 6:2230–2243. https://doi.org/10.1021/acscatal.5b02720
83. de Visser SP, Porro CS, Quesne MG et al (2013) Overview on theoretical studies discriminating the two-oxidant versus two-state-reactivity models for substrate monoxygenation by
cytochrome p450 enzymes. Curr Top Med Chem 13:2218–2232. https://doi.org/10.2174/
15680266113136660155
84. Forkert P-G, Lee RP (1997) Metabolism of ethyl carbamate by pulmonary cytochrome P450
and carboxylesterase isozymes: involvement of CYP2E1 and hydrolase A. Toxicol Appl
Pharmacol 146:245–254
85. Gunes A, Bilir E, Zengil H et al (2007) Inhibitory effect of valproic acid on cytochrome P450
2C9 activity in epilepsy patients. Basic Clin Pharmacol Toxicol 100:383–386
86. Lee RP, Parkinson A, Forkert PG (1998) Isozyme-selective metabolism of ethyl carbamate
by cytochrome P450 (CYP2E1) and carboxylesterase (hydrolase A) enzymes in murine liver
microsomes. Drug Metab Dispos 26:60–65
M. G. Quesne and S. P. de Visser
67. Gelb MH, Heimbrook DC, Malkonen P, Sligar SG (1982) Stereochemistry and deuterium isotope effects in camphor hydroxylation by the cytochrome P450cam monooxygenase system.
Biochemistry 21:370–377
68. Davydov DR, Hui Bon Hoa G, Peterson JA (1999) Dynamics of protein-bound water in the
heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam
and P450 2B4. Biochemistry 38:751–761
69. Ruettinger RT, Wen L-P, Fulco AJ (1989) Coding nucleotide, 5’regulatory, and deduced amino
acid sequences of P-450BM-3, a single peptide cytochrome P-450: NADPH-P-450 reductase
from Bacillus megaterium. J Biol Chem 264:10987–10995
70. Grogan G (2011) Cytochromes P450: exploiting diversity and enabling application as biocatalysts. Curr Opin Chem Biol 15:241–248
71. O’Reilly E, Köhler V, Flitsch SL, Turner NJ (2011) Cytochromes P450 as useful biocatalysts:
addressing the limitations. Chem Commun 47:2490–2501
72. Omura T, Sato R (1962) A new cytochrome in liver microsomes. J Biol Chem 237:PC1375PC1376
73. Auclair K, Moënne-Loccoz P, de Montellano PR (2001) Roles of the proximal heme thiolate
ligand in cytochrome P450cam. J Am Chem Soc 123:4877–4885
74. Poulos TL, Finzel BC, Gunsalus IC et al (1985) The 2.6-A crystal structure of Pseudomonas
putida cytochrome P-450. J Biol Chem 260:16122–16130
75. Schlichting I, Berendzen J, Chu K et al (2000) The catalytic pathway of cytochrome P450cam
at atomic resolution. Science (80-) 287:1615–1622
76. Rittle J, Green MT (2010) Cytochrome P450 compound I: capture, characterization, and CH
bond activation kinetics. Science (80-) 330:933–937
77. de Visser SP, Shaik S, Sharma PK et al (2003) Active species of horseradish peroxidase (HRP)
and cytochrome P450: two electronic chameleons. J Am Chem Soc 125:15779–15788. https://
doi.org/10.1021/ja0380906
78. Shaik S, Kumar D, de Visser SP et al (2005) Theoretical perspective on the structure and
mechanism of cytochrome P450 enzymes. Chem Rev 105:2279–2328. https://doi.org/10.
1021/cr030722j
79. Kamachi T, Yoshizawa K (2003) A theoretical study on the mechanism of camphor hydroxylation by compound I of cytochrome P450. J Am Chem Soc 125:4652–4661
80. de Visser SP, Ogliaro F, Shaik S (2001) 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 Cu. Angew Chem Int Ed Engl 40:2871–2874. DOI: https://doi.org/10.1002/15213773(20010803)40:15<2871::AID-ANIE2871>3.0.CO;2-R [pii]
81. Kumar D, de Visser SP, Sharma PK et al (2004) Radical clock substrates, their C-H hydroxylation mechanism by cytochrome P450, and other reactivity patterns: what does theory
reveal about the clocks’ behavior? J Am Chem Soc 126:1907–1920. https://doi.org/10.1021/
ja039439s
82. Quesne MG, Senthilnathan D, Singh D et al (2016) Origin of the enhanced reactivity of μnitrido-bridged diiron(IV)-Oxo porphyrinoid complexes over cytochrome P450 compound i.
ACS Catal 6:2230–2243. https://doi.org/10.1021/acscatal.5b02720
83. de Visser SP, Porro CS, Quesne MG et al (2013) Overview on theoretical studies discriminating the two-oxidant versus two-state-reactivity models for substrate monoxygenation by
cytochrome p450 enzymes. Curr Top Med Chem 13:2218–2232. https://doi.org/10.2174/
15680266113136660155
84. Forkert P-G, Lee RP (1997) Metabolism of ethyl carbamate by pulmonary cytochrome P450
and carboxylesterase isozymes: involvement of CYP2E1 and hydrolase A. Toxicol Appl
Pharmacol 146:245–254
85. Gunes A, Bilir E, Zengil H et al (2007) Inhibitory effect of valproic acid on cytochrome P450
2C9 activity in epilepsy patients. Basic Clin Pharmacol Toxicol 100:383–386
86. Lee RP, Parkinson A, Forkert PG (1998) Isozyme-selective metabolism of ethyl carbamate
by cytochrome P450 (CYP2E1) and carboxylesterase (hydrolase A) enzymes in murine liver
microsomes. Drug Metab Dispos 26:60–65