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• W4366754837 endingPage "112238" @default.
• W4366754837 startingPage "112238" @default.
• W4366754837 abstract "Human heme oxygenase-1 (hHO-1) plays a crucial role in human physiology because of its ability to metabolize free heme. The heme degradation products, biliverdin and bilirubin, were shown to have protective antioxidant properties in cells. In the context of cancer, hHO-1 function grants cancer cells defense from standard chemotherapy treatments, leading to the development of azole-based inhibitors that target hHO-1 for potential anticancer therapy. This work reports experimental and theoretical characterization of interactions between three azole-based inhibitors and the active site of hHO-1. It was found that all three compounds have Kd values within the μM order. The electronic absorption and resonance Raman (rR) spectra indicated that they bind to the ferric heme and coordinate through a nitrogen atom. rR measurements revealed varying effects of inhibitors on the geometry of heme vinyl groups in the ferric form of hHO-1. Changes in peripheral group orientation are known to affect heme redox potential, and consequently can reflect the inhibitory properties of studied azoles. The subsequent docking studies showed that inhibitors with lower Kd values are located close to two vinyl groups, while the compound with higher Kd is situated near only one, consistent with the rR studies. Finally, the rR studies of the CO adducts showed that the inhibitors bind to the heme in a reversible manner. Altogether, the combination of ligand binding studies, UV–Vis and rR spectroscopies, as well as computational approach revealed an importance of the steric hindrance imposed by the inhibitor's side chain." @default.
• W4366754837 created "2023-04-24" @default.
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• W4366754837 date "2023-07-01" @default.
• W4366754837 modified "2023-09-30" @default.
• W4366754837 title "Interactions of azole-based inhibitors with human heme oxygenase" @default.
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• W4366754837 doi "https://doi.org/10.1016/j.jinorgbio.2023.112238" @default.
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