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Related Experiment Video

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High Resolution Electron Microscopy of the Helicobacter pylori Cag Type IV Secretion System Pili Produced in Varying Conditions of Iron Availability

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Iron-containing urease in a pathogenic bacterium.

Eric L Carter¹, Dale E Tronrud, Scott R Taber

¹Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA.

Proceedings of the National Academy of Sciences of the United States of America

|July 27, 2011

Summary

This summary is machine-generated.

Helicobacter mustelae possesses a unique iron-urease, crucial for survival in nickel-poor environments. This enzyme

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Area of Science:

Microbiology
Biochemistry
Enzymology

Background:

Helicobacter mustelae is a gastric pathogen in ferrets.
It possesses both nickel-dependent and iron-dependent urease enzymes.

Purpose of the Study:

To characterize the distinct iron-dependent urease from Helicobacter mustelae.
To elucidate the structural and functional properties of this iron-urease.

Main Methods:

Spectroscopic analysis (electronic spectrum) of the oxidized iron-urease.
Biochemical assays to restore enzyme activity.
Structural analysis of the iron metallocenter.

Main Results:

The iron-urease is oxygen-labile and exhibits a methemerythrin-like spectrum when inactive.
Activity is restored upon reduction under anaerobic conditions.
Structural analysis reveals a dinuclear iron center bridged by lysine carbamate, similar to nickel-urease.

Conclusions:

Helicobacter mustelae synthesizes a functional iron-urease, compensating for low nickel availability.
This iron-urease is structurally analogous to nickel-urease active sites.
The enzyme's activity is vital for the pathogen's survival in the ferret's gastric environment.