Modified Active Site Coordination in a Clinical Mutant of Sulfite Oxidase

Authors

Christian J. Doonan, University of Saskatchewan
Heather L. Wilson, Duke University
K. V. Rajagopalan, Duke University
Robert M. Garrett, Duke University
Brian Bennett, Marquette UniversityFollow
Roger C. Prince, Exxon Mobil
Graham N. George, University of Saskatchewan

Document Type

Article

Language

eng

Format of Original

8 p.

Publication Date

8-2007

Publisher

American Chemical Society

Source Publication

Journal of the American Chemical Society

Source ISSN

0002-7863

Original Item ID

doi: 10.1021/ja071402a

Abstract

The molybdenum site of the Arginine 160 → Glutamine clinical mutant of the physiologically vital enzyme sulfite oxidase has been investigated by a combination of X-ray absorption spectroscopy and density functional theory calculations. We conclude that the mutant enzyme has a six-coordinate pseudo-octahedral active site with coordination of Glutamine O_ε to molybdenum. This contrasts with the wild-type enzyme which is five-coordinate with approximately square-based pyramidal geometry. This difference in the structure of the molybdenum site explains many of the properties of the mutant enzyme which have previously been reported.

Comments

Accepted version. Journal of the American Chemical Society, Vol. 129, No. 30 (August 2007): 9421-9428. DOI. © 2007 American Chemical Society. Used with permission.

Brian Bennett was affiliated with Medical College of Wisconsin at the time of publication.

Recommended Citation

Doonan, Christian J.; Wilson, Heather L.; Rajagopalan, K. V.; Garrett, Robert M.; Bennett, Brian; Prince, Roger C.; and George, Graham N., "Modified Active Site Coordination in a Clinical Mutant of Sulfite Oxidase" (2007). Physics Faculty Research and Publications. 24.
https://epublications.marquette.edu/physics_fac/24