Ontology highlight
ABSTRACT:
SUBMITTER: Geng J
PROVIDER: S-EPMC3683780 | biostudies-literature | 2013 Jun
REPOSITORIES: biostudies-literature
Geng Jiafeng J Dornevil Kednerlin K Davidson Victor L VL Liu Aimin A
Proceedings of the National Academy of Sciences of the United States of America 20130529 24
The diheme enzyme MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor protein to generate a tryptophan tryptophylquinone cofactor. The MauG-catalyzed reaction proceeds via a bis-Fe(IV) intermediate in which one heme is present as Fe(IV)=O and the other as Fe(IV) with axial histidine and tyrosine ligation. Herein, a unique near-infrared absorption feature exhibited specifically in bis-Fe(IV) MauG is described, and evidence is presented that it results from a ch ...[more]