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https://hdl.handle.net/2440/47090
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dc.contributor.author | Harris, H. | - |
dc.contributor.author | George, G. | - |
dc.contributor.author | Rajagopalan, K. | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Inorganic Chemistry: including bioinorganic chemistry, 2006; 45(2):493-495 | - |
dc.identifier.issn | 0020-1669 | - |
dc.identifier.issn | 1520-510X | - |
dc.identifier.uri | http://hdl.handle.net/2440/47090 | - |
dc.description | Copyright © 2005 American Chemical Society | - |
dc.description.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. | - |
dc.description.statementofresponsibility | Hugh H. Harris, Graham N. George, and K. V. Rajagopalan | - |
dc.language.iso | en | - |
dc.publisher | Amer Chemical Soc | - |
dc.source.uri | http://pubs.acs.org/cgi-bin/abstract.cgi/inocaj/2006/45/i02/abs/ic0512274.html | - |
dc.subject | Humans | - |
dc.subject | Crystallography, X-Ray | - |
dc.subject | Spectrum Analysis | - |
dc.subject | Sensitivity and Specificity | - |
dc.subject | Binding Sites | - |
dc.subject | Quantum Theory | - |
dc.subject | X-Rays | - |
dc.subject | Models, Chemical | - |
dc.subject | Sulfite Oxidase | - |
dc.title | High-resolution EXAFS of the active site of human sulfite oxidase: Comparison with density functional theory and X-ray crystallographic results | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1021/ic0512274 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Harris, H. [0000-0002-3472-8628] | - |
Appears in Collections: | Aurora harvest Chemistry and Physics publications Environment Institute publications |
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