Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||High-resolution EXAFS of the active site of human sulfite oxidase: Comparison with density functional theory and X-ray crystallographic results|
|Citation:||Inorganic Chemistry, 2006; 45(2):493-495|
|Publisher:||Amer Chemical Soc|
|Hugh H. Harris, Graham N. George, and K. V. Rajagopalan|
|Abstract:||Much of our knowledge about molybdenum enzymes has originated from EXAFS spectroscopy. This technique provides excellent bond-length accuracy but has only limited bond-length resolution. We have used EXAFS spectroscopy with an extended data range in an attempt to improve bond-length resolution for the molybdenum enzyme sulfite oxidase. The Mo site of sulfite oxidase has two oxygen and three Mo-S ligands (two from cofactor dithiolene plus a cysteine). For the oxidized (Mo(VI)) enzyme, we find that the three Mo-S bond lengths are very similar (within 0.05 A) at 2.41 A, as are the Mo=O ligands at 1.72 A. Density functional theory shows that this is consistent with the proposed active-site structure. The reduced (Mo(IV)) enzyme shows two Mo-S bond lengths at 2.35 A and one at 2.41 A (assigned to cofactor dithiolene and cysteine, respectively, from DFT), together with one Mo=O at 1.72 A and one Mo-OH(2) at 2.30 A.|
|Keywords:||Humans; Crystallography, X-Ray; Spectrum Analysis; Sensitivity and Specificity; Binding Sites; Quantum Theory; X-Rays; Models, Chemical; Sulfite Oxidase|
|Description:||Copyright © 2005 American Chemical Society|
|Appears in Collections:||Chemistry and Physics publications|
Environment Institute publications
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.