Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/47090
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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, 2006; 45(2):493-495
Publisher: Amer Chemical Soc
Issue Date: 2006
ISSN: 0020-1669
1520-510X
Statement of
Responsibility: 
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
RMID: 0020081438
DOI: 10.1021/ic0512274
Published version: http://pubs.acs.org/cgi-bin/abstract.cgi/inocaj/2006/45/i02/abs/ic0512274.html
Appears in Collections:Chemistry and Physics publications
Environment Institute publications

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