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Iron-containing urease in a pathogenic bacterium.


ABSTRACT: 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 metallocenter bridged by a lysine carbamate, closely resembling the traditional nickel-urease active site. Although the iron-urease is less active than the nickel-enzyme, its activity allows H. mustelae to survive the carnivore's low-nickel gastric environment.

SUBMITTER: Carter EL 

PROVIDER: S-EPMC3156221 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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Iron-containing urease in a pathogenic bacterium.

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]

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