Cytochromes P450 (CYPs) are superfamily of oxidoreductases with a hem-thiolate moiety. CYPs catalyze hydroxylation and some other oxidation reactions, including C-N, C-O and C-C bond cleavage. Their biological functions include xenobiotic detoxification and biosynthesis of hormone and other bioregulators using hydrophobic substrates like steroid and fatty acids. Coumarin derivatives are known to be substrates or inhibitors for some CYPs [1], but due to high amounts of coumarins and CYPs exist, some interactions of particular CYP-coumarin pairs is still undetermined. In this paper we report about of synthesis of 7-hydroxycoumarin-4-acetic acid (7-hydroxy-4-methyl-2H-chroman2-one, Pubchem ID CID: 5338490) using published method [2]. The product was found to by pure according to TLC assay and absorbance maxima at 320 and 365 nm in HCl acidified and K₂CO₃-buffered water:ethanol (10 : 1, v:v), respectively. To evaluate in silico its possible interactions with CYPs Autodock Vina (AV) together with authored helper software FYTdock [3] for highthroughput virtual screening (HTVS) were used together with majority of 3D structures of CYPs from PDB database. It was found that affine binding with AV scores in range -9 - -9.4 were found for human CYP1A1 structure (PDB code 6DWM), bacterial P450-BM3 (3BEN), OleT (5M0N, 4L40, 4L54), CYP260A1 S276I mutant (6F8C) and P450-CAM (1PHE). To the best of our knowledge the interactions have not been reported yet even in silico. Our results indicate on possibility to check such interactions in vitro, e.g. to develop fluorescence-based screening system for the aforementioned enzymes.