Literature summary for 1.8.5.3 extracted from

George, G.; Doonan, C.; Rothery, R.; Boroumand, N.; Weiner, J.
X-ray absorption spectroscopic characterization of the molybdenum site of Escherichia coli dimethyl sulfoxide reductase (2007), Inorg. Chem., 46, 2-4.

Crystallization (Commentary)

Crystallization (Comment)	Organism
X-ray absorption spectroscopic analysis of the molybdenum active site of Escherichia coli dimethyl sulfoxide reductase contained within its native membranes.The oxidized active site has four Mo-S ligands at 2.43 A, one Mo=O at 1.71 A, and a longer Mo-O at 1.90 A. The oxidized enzyme is a monooxomolybdenum(VI) species coordinated by two molybdopterin dithiolenes and a serine. Results suggest that the form found in vivo is the monooxobis(molybdopterin) species	Escherichia coli

Crystallization (Comment)

Organism

X-ray absorption spectroscopic analysis of the molybdenum active site of Escherichia coli dimethyl sulfoxide reductase contained within its native membranes.The oxidized active site has four Mo-S ligands at 2.43 A, one Mo=O at 1.71 A, and a longer Mo-O at 1.90 A. The oxidized enzyme is a monooxomolybdenum(VI) species coordinated by two molybdopterin dithiolenes and a serine. Results suggest that the form found in vivo is the monooxobis(molybdopterin) species

Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Molybdenum	the oxidized active site has four Mo-S ligands at 2.43 A, one Mo=O at 1.71 A, and a longer Mo-O at 1.90 A. The oxidized enzyme is a monooxomolybdenum(VI) species coordinated by two molybdopterin dithiolenes and a serine. Results suggest that the form found in vivo is the monooxobis(molybdopterin) species	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)