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Type: Journal article
Title: High-resolution EXAFS of the active site of human sulfite oxidase: Comparison with density functional theory and X-ray crystallographic results
Author: Harris, H.
George, G.
Rajagopalan, K.
Citation: Inorganic Chemistry: including bioinorganic chemistry, 2006; 45(2):493-495
Publisher: Amer Chemical Soc
Issue Date: 2006
ISSN: 0020-1669
Statement of
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
Models, Chemical
Sulfite Oxidase
Description: Copyright © 2005 American Chemical Society
DOI: 10.1021/ic0512274
Published version:
Appears in Collections:Aurora harvest
Chemistry and Physics publications
Environment Institute publications

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