Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/66163
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Type: Journal article
Title: X-ray absorption spectroscopic characterization of the molybdenum site of Escherichia coli dimethyl sulfoxide reductase
Author: George, G.
Doonan, C.
Rothery, R.
Boroumand, N.
Weiner, J.
Citation: Inorganic Chemistry: including bioinorganic chemistry, 2007; 46(1):2-4
Publisher: Amer Chemical Soc
Issue Date: 2007
ISSN: 0020-1669
1520-510X
Statement of
Responsibility: 
Graham N. George, Christian J. Doonan, Richard A. Rothery, Nasim Boroumand and Joel H. Weiner
Abstract: Structural studies of dimethyl sulfoxide (DMSO) reductases were hampered by modification of the active site during purification. We report an X-ray absorption spectroscopic analysis of the molybdenum active site of Escherichia coli DMSO reductase contained within its native membranes. The enzyme in these preparations is expected to be very close to the form found in vivo. The oxidized active site was found to have four Mo-S ligands at 2.43 A, one Mo=O at 1.71 A, and a longer Mo-O at 1.90 A. We conclude that the oxidized enzyme is a monooxomolybdenum(VI) species coordinated by two molybdopterin dithiolenes and a serine. The bond lengths determined for E. coli DMSO reductase are very similar to those determined for the well-characterized Rhodobacter sphaeroides DMSO reductase, suggesting similar active site structures for the two enzymes. Furthermore, our results suggest that the form found in vivo is the monooxobis(molybdopterin) species.
Keywords: Escherichia coli
Molybdenum
Oxidoreductases
Iron-Sulfur Proteins
Spectrum Analysis
Binding Sites
Molecular Structure
X-Rays
Rights: Copyright © 2007 American Chemical Society
DOI: 10.1021/ic061695t
Appears in Collections:Aurora harvest
Chemistry publications
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