Format of Original
American Chemical Society
Journal of the American Chemical Society
Original Item ID
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 Oε 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.
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.