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Initial Steps to Engineer Coproheme Decarboxylase to Obtain Stereospecific Monovinyl, Monopropionyl Deuterohemes.


ABSTRACT: The oxidative decarboxylation of coproheme to form heme b by coproheme decarboxylase is a stereospecific two-step reaction. In the first step, the propionate at position two (p2) is cleaved off the pyrrole ring A to form a vinyl group at this position. Subsequently, the propionate at position four (p4) on pyrrole ring B is cleaved off and heme b is formed. In this study, we attempted to engineer coproheme decarboxylase from Corynebacterium diphtheriae to alter the stereospecificity of this reaction. By introducing a tyrosine residue in proximity to the propionate at position 4, we were able to create a new radical center in the active site. However, the artificial Tyr183 radical could not be shown to catalyze any decarboxylation.

SUBMITTER: Michlits H 

PROVIDER: S-EPMC8819088 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature

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Initial Steps to Engineer Coproheme Decarboxylase to Obtain Stereospecific Monovinyl, Monopropionyl Deuterohemes.

Michlits Hanna H   Valente Nina N   Mlynek Georg G   Hofbauer Stefan S  

Frontiers in bioengineering and biotechnology 20220124


The oxidative decarboxylation of coproheme to form heme <i>b</i> by coproheme decarboxylase is a stereospecific two-step reaction. In the first step, the propionate at position two (p2) is cleaved off the pyrrole ring A to form a vinyl group at this position. Subsequently, the propionate at position four (p4) on pyrrole ring B is cleaved off and heme <i>b</i> is formed. In this study, we attempted to engineer coproheme decarboxylase from <i>Corynebacterium diphtheriae</i> to alter the stereospec  ...[more]

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