Promiscuity in Molecular Mimics of the Cysteine Dioxygenase: Effects of Selenium in the Substrate and Cobalt as the Central Metal Ion.

ABSTRACT: Cysteine dioxygenase (CDO) catalyzes the conversion of cysteine with dioxygen to yield cysteine sulfinic acid, which lies at the branching point of cysteine catabolism. Despite many years of research there are still many questions related to its functioning. Thus, CDO is inactive with selenocysteine (Sec) or when the central iron ion is replaced by cobalt. In this context, we report here biomimetic CDO models with bound selenocysteamine substrate ligands, namely [Tp^MesFe(Se-CH₂-CH₂-NH₂)] and [Tp^Mes*Fe(Se-CH₂-CH₂-NH₂)] (with Tp^Mes = hydrotris(3-mesitylpyrazol-1-yl)borate, Tp^Mes* = hydrobis((3-mesitylpyrazol-1-yl)(5-mesitylpyrazol-1-yl)borate) and in addition a cobalt-analogue [Tp

SUBMITTER: Weißer K 

PROVIDER: S-EPMC12462750 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature