Ontology highlight
ABSTRACT:
SUBMITTER: Carter EL
PROVIDER: S-EPMC3156221 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
Carter Eric L EL Tronrud Dale E DE Taber Scott R SR Karplus P Andrew PA Hausinger Robert P RP
Proceedings of the National Academy of Sciences of the United States of America 20110725 32
Helicobacter mustelae, a gastric pathogen of ferrets, synthesizes a distinct iron-dependent urease in addition to its archetypical nickel-containing enzyme. The iron-urease is oxygen-labile, with the inactive protein exhibiting a methemerythrin-like electronic spectrum. Significantly, incubation of the oxidized protein with dithionite under anaerobic conditions leads to restoration of activity and bleaching of the spectrum. Structural analysis of the oxidized species reveals a dinuclear iron met ...[more]