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https://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: including bioinorganic 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 |
DOI: | 10.1021/ic0512274 |
Published version: | http://pubs.acs.org/cgi-bin/abstract.cgi/inocaj/2006/45/i02/abs/ic0512274.html |
Appears in Collections: | Aurora harvest Chemistry and Physics publications Environment Institute publications |
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