Spectroscopic Investigation of Cysteamine Dioxygenase.

ABSTRACT: Thiol dioxygenases are mononuclear non-heme Fe^II-dependent metalloenzymes that initiate the oxidative catabolism of thiol-containing substrates to their respective sulfinates. Cysteine dioxygenase (CDO), the best characterized mammalian thiol dioxygenase, contains a three-histidine (3-His) coordination environment rather than the 2-His-1-carboxylate facial triad seen in most mononuclear non-heme Fe^II enzymes. A similar 3-His active site is found in the bacterial thiol dioxygenase 3-mercaptopropionate dioxygenase (MDO), which converts 3-mercaptopropionate into 3-sulfinopropionic acid as part of the bacterial sulfur metabolism pathway. In this study, we have investigated the active site geometric and electronic structures of a third non-heme Fe^II-dependent th

SUBMITTER: Fernandez RL 

PROVIDER: S-EPMC7717700 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature