Title : How do azoles inhibit cytochrome P450 enzymes? A density functional study.

Pub. Date : 2008 Dec 18

PMID : 18563875






2 Functional Relationships(s)
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1 Studies with an extra hydrogen-bonded ethanol molecule in the model, mimicking the active site of the CYP121 P450, show that the resting state and azole binding structures are close in energy, which may lead to chemical equilibrium between the two structures, as indeed observed with recent protein structural studies that have demonstrated two distinct azole binding mechanisms to P450 heme. Hydrogen cytochrome P450 family 2 subfamily B member 6 Homo sapiens
2 Studies with an extra hydrogen-bonded ethanol molecule in the model, mimicking the active site of the CYP121 P450, show that the resting state and azole binding structures are close in energy, which may lead to chemical equilibrium between the two structures, as indeed observed with recent protein structural studies that have demonstrated two distinct azole binding mechanisms to P450 heme. Hydrogen cytochrome P450 family 2 subfamily B member 6 Homo sapiens