The Quest for Accurate Theoretical Models of Metalloenzymes …
459
46. Hernández-Ortega A, Quesne MG, Bui S et al (2015) Catalytic mechanism of cofactor-free
dioxygenases and how they circumvent spin-forbidden oxygenation of their substrates. J Am
Chem Soc 137:7474–7487. https://doi.org/10.1021/jacs.5b03836
47. Lee C, Yang W, Parr RG (1988) Development of the Colle-Salvetti correlation-energy formula
into a functional of the electron density. Phys Rev B 37:785
48. Smith W, Yong CW, Rodger PM (2002) DL_POLY: application to molecular simulation. Mol
Simul 28:385–471
49. Ahlrichs R, Bar M, Haser M et al (1989) Chem Phys Lett 162:165. Curr version see. https://
www.turbomole.com
50. Thierbach S, Bui N, Zapp J et al (2014) Substrate-Assisted O2 activation in a cofactorindependent dioxygenase. Chem Biol 21:217–225. https://doi.org/10.1016/J.CHEMBIOL.
2013.11.013
51. Pratter SM, Konstantinovics C, Di Giuro CML et al (2013) inversion of enantioselectivity of
a mononuclear non-heme iron (II)-dependent hydroxylase by tuning the interplay of metalcenter geometry and protein structure. Angew Chemie 125:9859–9863
52. de Visser SP (2006) Propene activation by the oxo-iron active species of taurine/alphaketoglutarate dioxygenase (TauD) enzyme. How does the catalysis compare to hemeenzymes? J Am Chem Soc 128:9813–9824. https://doi.org/10.1021/ja061581g
53. Latifi R, Bagherzadeh M, de Visser SP (2009) 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 (Easton) 15:6651–6662. https://doi.org/
10.1002/chem.200900211
54. Karamzadeh B, Kumar D, Sastry GN, de Visser SP (2010) Steric factors override thermodynamic driving force in regioselectivity of proline hydroxylation by prolyl-4-hydroxylase
enzymes. J Phys Chem A 114:13234–13243. https://doi.org/10.1021/jp1089855
55. Faponle AS, Seebeck FP, de Visser SP (2017) Sulfoxide synthase versus cysteine dioxygenase
reactivity in a nonheme iron enzyme. J Am Chem Soc 139:9259–9270. https://doi.org/10.
1021/jacs.7b04251
56. de Montellano PRO (2010) Hydrocarbon hydroxylation by cytochrome P450 enzymes. Chem
Rev 110:932
57. de Montellano PRO (2004) Cytochrome P450: structure, mechanism, and biochemistry.
Springer
58. Denisov IG, Makris TM, Sligar SG, Schlichting I (2005) Structure and chemistry of
cytochrome P450. Chem Rev 105:2253–2277. https://doi.org/10.1021/cr0307143
59. Groves JT (2003) The bioinorganic chemistry of iron in oxygenases and supramolecular
assemblies. Proc Natl Acad Sci 100:3569–3574. https://doi.org/10.1073/pnas.0830019100
60. Kadish KM, Smith KM, Guilard R (2010) Handbook of porphyrin science. World Scientific
61. Ji L, Faponle AS, Quesne MG et al (2015) Drug metabolism by cytochrome P450 enzymes:
what distinguishes the pathways leading to substrate hydroxylation over desaturation?
Chem—A Eur J 21:9083–9092. https://doi.org/10.1002/chem.201500329
62. Reinhard FC, de Visser S (2017) Biodegradation of cosmetics products: a computational
study of cytochrome P450 metabolism of phthalates. Inorganics 5:77. https://doi.org/10.3390/
inorganics5040077
63. Guengerich FP (2001) Common and uncommon cytochrome P450 reactions related to
metabolism and chemical toxicity. Chem Res Toxicol 14:611–650
64. Munro AW, Girvan HM, McLean KJ (2007) Variations on a (t) heme–novel mechanisms,
redox partners and catalytic functions in the cytochrome P450 superfamily. Nat Prod Rep
24:585–609
65. Posner GH, O’Neill PM (2004) Knowledge of the proposed chemical mechanism of action
and cytochrome P450 metabolism of antimalarial trioxanes like artemisinin allows rational
design of new antimalarial peroxides. Acc Chem Res 37:397–404
66. Atkins WM, Sligar SG (1987) Metabolic switching in cyctochrome P-450cam: deuterium
isotope effects on regiospecificity and the monooxygenase/oxidase ratio. J Am Chem Soc
109:3754–3760
459
46. Hernández-Ortega A, Quesne MG, Bui S et al (2015) Catalytic mechanism of cofactor-free
dioxygenases and how they circumvent spin-forbidden oxygenation of their substrates. J Am
Chem Soc 137:7474–7487. https://doi.org/10.1021/jacs.5b03836
47. Lee C, Yang W, Parr RG (1988) Development of the Colle-Salvetti correlation-energy formula
into a functional of the electron density. Phys Rev B 37:785
48. Smith W, Yong CW, Rodger PM (2002) DL_POLY: application to molecular simulation. Mol
Simul 28:385–471
49. Ahlrichs R, Bar M, Haser M et al (1989) Chem Phys Lett 162:165. Curr version see. https://
www.turbomole.com
50. Thierbach S, Bui N, Zapp J et al (2014) Substrate-Assisted O2 activation in a cofactorindependent dioxygenase. Chem Biol 21:217–225. https://doi.org/10.1016/J.CHEMBIOL.
2013.11.013
51. Pratter SM, Konstantinovics C, Di Giuro CML et al (2013) inversion of enantioselectivity of
a mononuclear non-heme iron (II)-dependent hydroxylase by tuning the interplay of metalcenter geometry and protein structure. Angew Chemie 125:9859–9863
52. de Visser SP (2006) Propene activation by the oxo-iron active species of taurine/alphaketoglutarate dioxygenase (TauD) enzyme. How does the catalysis compare to hemeenzymes? J Am Chem Soc 128:9813–9824. https://doi.org/10.1021/ja061581g
53. Latifi R, Bagherzadeh M, de Visser SP (2009) 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 (Easton) 15:6651–6662. https://doi.org/
10.1002/chem.200900211
54. Karamzadeh B, Kumar D, Sastry GN, de Visser SP (2010) Steric factors override thermodynamic driving force in regioselectivity of proline hydroxylation by prolyl-4-hydroxylase
enzymes. J Phys Chem A 114:13234–13243. https://doi.org/10.1021/jp1089855
55. Faponle AS, Seebeck FP, de Visser SP (2017) Sulfoxide synthase versus cysteine dioxygenase
reactivity in a nonheme iron enzyme. J Am Chem Soc 139:9259–9270. https://doi.org/10.
1021/jacs.7b04251
56. de Montellano PRO (2010) Hydrocarbon hydroxylation by cytochrome P450 enzymes. Chem
Rev 110:932
57. de Montellano PRO (2004) Cytochrome P450: structure, mechanism, and biochemistry.
Springer
58. Denisov IG, Makris TM, Sligar SG, Schlichting I (2005) Structure and chemistry of
cytochrome P450. Chem Rev 105:2253–2277. https://doi.org/10.1021/cr0307143
59. Groves JT (2003) The bioinorganic chemistry of iron in oxygenases and supramolecular
assemblies. Proc Natl Acad Sci 100:3569–3574. https://doi.org/10.1073/pnas.0830019100
60. Kadish KM, Smith KM, Guilard R (2010) Handbook of porphyrin science. World Scientific
61. Ji L, Faponle AS, Quesne MG et al (2015) Drug metabolism by cytochrome P450 enzymes:
what distinguishes the pathways leading to substrate hydroxylation over desaturation?
Chem—A Eur J 21:9083–9092. https://doi.org/10.1002/chem.201500329
62. Reinhard FC, de Visser S (2017) Biodegradation of cosmetics products: a computational
study of cytochrome P450 metabolism of phthalates. Inorganics 5:77. https://doi.org/10.3390/
inorganics5040077
63. Guengerich FP (2001) Common and uncommon cytochrome P450 reactions related to
metabolism and chemical toxicity. Chem Res Toxicol 14:611–650
64. Munro AW, Girvan HM, McLean KJ (2007) Variations on a (t) heme–novel mechanisms,
redox partners and catalytic functions in the cytochrome P450 superfamily. Nat Prod Rep
24:585–609
65. Posner GH, O’Neill PM (2004) Knowledge of the proposed chemical mechanism of action
and cytochrome P450 metabolism of antimalarial trioxanes like artemisinin allows rational
design of new antimalarial peroxides. Acc Chem Res 37:397–404
66. Atkins WM, Sligar SG (1987) Metabolic switching in cyctochrome P-450cam: deuterium
isotope effects on regiospecificity and the monooxygenase/oxidase ratio. J Am Chem Soc
109:3754–3760