Investigation of Spin-Charge-Structure in Human Verdoheme Using TheDFT Method

The enzyme heme oxygenase (HO) plays an essential role in the destruction of hememolecules. Heme oxygenase uses dioxygen to open the specific orientation of the porphyrin ringat the position of the α-meso carbon.This enzyme catalyses the degradation of heme to biliverdinIXα through three distinct intermediates, α-hydroxyheme, α-verdoheme and ferric biliverdin–Iron chelate, at the expense of O۲ and electrons. To elucidate the mysterious mechanism of theoxygenation steps, the atomic-resolution structure of the verdoheme–HO complex has beenneeded. In this work the structure of Iron verdoheme in complex with Human Heme Oxygenaseaccording to the structure of verdoheme that was solved by Lad et all (PDB Id: ۱TWN) (figure۲), was studied by density functional theory based B۳LYP method and ۶-۳۱G basis set. Hereinwe regard the central metal of the five coordinated human verdoheme as ferrous (Fe۲+) andferric (Fe۳+).Many parameters such as charge of verdoheme and Iron as central metal, electrondistribution, spin multiplicity of the molecule and proximal substituents effect on the verdohemering stabilization and their arrangement were discussed

Keywords:

Verdoheme , Human , Density Functional Theory , structure optimization