Modified active site coordination in a clinical mutant of sulfite oxidase. J Am Chem Soc 2007 Aug 01;129(30):9421-8
Date
07/05/2007Pubmed ID
17608478DOI
10.1021/ja071402aScopus ID
2-s2.0-34547675920 (requires institutional sign-in at Scopus site) 29 CitationsAbstract
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 Oepsilon 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.
Author List
Doonan CJ, Wilson HL, Rajagopalan KV, Garrett RM, Bennett B, Prince RC, George GNAuthor
Brian Bennett D.Phil. Professor and Chair in the Physics department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
AlgorithmsArginine
Binding Sites
Computer Simulation
Crystallography, X-Ray
Glutamine
Hydrogen-Ion Concentration
Molybdenum
Mutation
Organometallic Compounds
Protein Conformation
Spectrum Analysis
Sulfite Oxidase
X-Rays
