The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Ebbe Nordlander. Portrait.

Ebbe Nordlander

Professor

Ebbe Nordlander. Portrait.

Computational modeling of the mechanism of urease.

Author

  • Håkan Carlsson
  • Ebbe Nordlander

Summary, in English

In order to elucidate aspects of the mechanism of the hydrolytic enzyme urease, theoretical calculations were undertaken on a model of the active site, using density functional theory. The bridging oxygen donor that has been found in the crystal structures was determined to be a hydroxide ion. The initial coordination of urea at the active site occurs most likely through the urea oxygen to the nickel ion with the lowest coordination number. This coordination can be made without much gain in energy. The calculations also showed that weak coordination of one of the urea amine nitrogen atoms to the second nickel atom is energetically feasible. Furthermore, a proposed mechanism including a tetrahedral intermediate generated by hydrolytic attack on the urea carbon by the bridging hydroxide was modeled, and the tetrahedral intermediate was found to be energetically unfavorable relative to terminal coordination of the substrate (urea).

Department/s

  • Department of Chemistry
  • Chemical Physics

Publishing year

2010

Language

English

Publication/Series

Bioinorganic Chemistry and Applications

Volume

2010

Document type

Journal article

Publisher

Hindawi Limited

Topic

  • Atom and Molecular Physics and Optics

Status

Published

ISBN/ISSN/Other

  • ISSN: 1687-479X