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

Pub. Date : 2006 May 12

PMID : 16563352






8 Functional Relationships(s)
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1 Binding of bufuralol, dextromethorphan, and 3,4-methylenedioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy. N-Methyl-3,4-methylenedioxyamphetamine cytochrome P450 family 2 subfamily D member 6 Homo sapiens
2 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). N-Methyl-3,4-methylenedioxyamphetamine cytochrome P450 family 2 subfamily D member 6 Homo sapiens
3 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). N-Methyl-3,4-methylenedioxyamphetamine cytochrome P450 family 2 subfamily D member 6 Homo sapiens
4 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). N-Methyl-3,4-methylenedioxyamphetamine cytochrome P450 family 2 subfamily D member 6 Homo sapiens
5 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). N-Methyl-3,4-methylenedioxyamphetamine cytochrome P450 family 2 subfamily D member 6 Homo sapiens
6 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. N-Methyl-3,4-methylenedioxyamphetamine cytochrome P450 family 2 subfamily D member 6 Homo sapiens
7 Spectra of the F120A mutant CYP2D6 suggest that Phe120 is involved in substrate-binding of dextromethorphan and MDMA, being responsible for the spectral differences observed between these two compounds and bufuralol. N-Methyl-3,4-methylenedioxyamphetamine cytochrome P450 family 2 subfamily D member 6 Homo sapiens
8 These differences could be explained postulating a different substrate mobility for each compound in the CYP2D6 active site, consistently with the role previously suggested for Phe120 in binding dextromethorphan and MDMA. N-Methyl-3,4-methylenedioxyamphetamine cytochrome P450 family 2 subfamily D member 6 Homo sapiens