Binding of bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy

A. Bonifacio; P.H.J. Keizers; J.N.M. Commandeur; N.P.E. Vermeulen; B. Robert; C. Gooijer; G. van der Zwan

doi:10.1016/j.bbrc.2006.03.027

Binding of bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy

A. Bonifacio
, P.H.J. Keizers
, J.N.M. Commandeur
, N.P.E. Vermeulen
, B. Robert
, C. Gooijer
, G. van der Zwan

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Cytochrome P450 2D6 (CYP2D6) is one of the most important drug-metabolizing enzymes in humans. Resonance Raman data, reported for the first time for CYP2D6, show that the CYP2D6 heme is found to be in a six-coordinated low-spin state in the absence of substrates, and it is perturbed to different extents by bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine (MDMA). Dextromethorphan and MDMA induce in CYP2D6 a significant amount of five-coordinated high-spin heme species and reduce the polarity of its heme-pocket, whereas bufuralol does not. Spectra of the F120A mutant CYP2D6 suggest that Phe

Original language	English
Pages (from-to)	772-9
Journal	Biochemical and Biophysical Research Communications
Volume	343
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2006.03.027
Publication status	Published - 2006

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This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

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10.1016/j.bbrc.2006.03.027

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Bonifacio, A., Keizers, P. H. J., Commandeur, J. N. M., Vermeulen, N. P. E., Robert, B., Gooijer, C., & van der Zwan, G. (2006). Binding of bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy. Biochemical and Biophysical Research Communications, 343(3), 772-9. https://doi.org/10.1016/j.bbrc.2006.03.027

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title = "Binding of bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy",

abstract = "Cytochrome P450 2D6 (CYP2D6) is one of the most important drug-metabolizing enzymes in humans. Resonance Raman data, reported for the first time for CYP2D6, show that the CYP2D6 heme is found to be in a six-coordinated low-spin state in the absence of substrates, and it is perturbed to different extents by bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine (MDMA). Dextromethorphan and MDMA induce in CYP2D6 a significant amount of five-coordinated high-spin heme species and reduce the polarity of its heme-pocket, whereas bufuralol does not. Spectra of the F120A mutant CYP2D6 suggest that Phe",

author = "A. Bonifacio and P.H.J. Keizers and J.N.M. Commandeur and N.P.E. Vermeulen and B. Robert and C. Gooijer and \{van der Zwan\}, G.",

year = "2006",

doi = "10.1016/j.bbrc.2006.03.027",

language = "English",

volume = "343",

pages = "772--9",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

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}

Bonifacio, A, Keizers, PHJ, Commandeur, JNM, Vermeulen, NPE, Robert, B, Gooijer, C & van der Zwan, G 2006, 'Binding of bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy', Biochemical and Biophysical Research Communications, vol. 343, no. 3, pp. 772-9. https://doi.org/10.1016/j.bbrc.2006.03.027

Binding of bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy. / Bonifacio, A.; Keizers, P.H.J.; Commandeur, J.N.M. et al.
In: Biochemical and Biophysical Research Communications, Vol. 343, No. 3, 2006, p. 772-9.

Research output: Contribution to Journal › Article › Academic › peer-review

TY - JOUR

T1 - Binding of bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy

AU - Bonifacio, A.

AU - Keizers, P.H.J.

AU - Commandeur, J.N.M.

AU - Vermeulen, N.P.E.

AU - Robert, B.

AU - Gooijer, C.

AU - van der Zwan, G.

PY - 2006

Y1 - 2006

N2 - Cytochrome P450 2D6 (CYP2D6) is one of the most important drug-metabolizing enzymes in humans. Resonance Raman data, reported for the first time for CYP2D6, show that the CYP2D6 heme is found to be in a six-coordinated low-spin state in the absence of substrates, and it is perturbed to different extents by bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine (MDMA). Dextromethorphan and MDMA induce in CYP2D6 a significant amount of five-coordinated high-spin heme species and reduce the polarity of its heme-pocket, whereas bufuralol does not. Spectra of the F120A mutant CYP2D6 suggest that Phe

AB - Cytochrome P450 2D6 (CYP2D6) is one of the most important drug-metabolizing enzymes in humans. Resonance Raman data, reported for the first time for CYP2D6, show that the CYP2D6 heme is found to be in a six-coordinated low-spin state in the absence of substrates, and it is perturbed to different extents by bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine (MDMA). Dextromethorphan and MDMA induce in CYP2D6 a significant amount of five-coordinated high-spin heme species and reduce the polarity of its heme-pocket, whereas bufuralol does not. Spectra of the F120A mutant CYP2D6 suggest that Phe

U2 - 10.1016/j.bbrc.2006.03.027

DO - 10.1016/j.bbrc.2006.03.027

M3 - Article

SN - 0006-291X

VL - 343

SP - 772

EP - 779

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Binding of bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy

Abstract

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