Structure of the molybdenum site of Escherichia coli trimethylamine N-oxide reductase.
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.
Zhang
Limei
L
Department of Geological Sciences, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E2, Canada.
Nelson
Kimberly Johnson
KJ
Rajagopalan
K V
KV
George
Graham N
GN
D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors