Reorienting Mechanism of Harderoheme in Coproheme Decarboxylase-A Computational Study.

ABSTRACT: Coproheme decarboxylase (ChdC) is an important enzyme in the coproporphyrin-dependent pathway (CPD) of Gram-positive bacteria that decarboxylates coproheme on two propionates at position 2 and position 4 sequentially to generate heme b by using H₂O₂ as an oxidant. This work focused on the ChdC from Geobacillus stearothermophilus (GsChdC) to elucidate the mechanism of its sequential two-step decarboxylation of coproheme. The models of GsChdC in a complex with substrate and reaction intermediate were built to investigate the reorienting mechanism of harderoheme. Targeted molecular dynamics simulations on these models validated that harderoheme is able to rotate in the active site of GsChdC with a 19.06-kcal·mol^-1 energy barrier after the first step of

SUBMITTER: Liu W 

PROVIDER: S-EPMC8910490 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature