Structure of the Molybdenum Site of EEcherichia Coli Trimethylamine N-Oxide Reductase
Journal Article
·
· Inorg. Chem 47:1074,2008
OSTI ID:953526
We report a structural characterization of the molybdenum site of recombinant Escherichia coli trimethylamine N-oxide (TMAO) reductase using X-ray absorption spectroscopy. The enzyme active site shows considerable similarity to that of dimethyl sulfoxide (DMSO) reductase, in that, like DMSO reductase, the TMAO reductase active site can exist in multiple forms. Examination of the published crystal structure of TMAO oxidase from Shewanella massilia indicates that the postulated Mo coordination structure is chemically impossible. The presence of multiple active site structures provides a potential explanation for the anomalous features reported from the crystal structure.
- Research Organization:
- SLAC National Accelerator Lab., Menlo Park, CA (United States)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC02-76SF00515
- OSTI ID:
- 953526
- Report Number(s):
- SLAC-REPRINT-2009-357; INOCAJ; TRN: US201002%%1354
- Journal Information:
- Inorg. Chem 47:1074,2008, Vol. 47, Issue 3; ISSN 0020-1669
- Country of Publication:
- United States
- Language:
- English
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