Molybdenum Incorporation in Tungsten Aldehyde Oxidoreductase Enzymes from Pyrococcus furiosus
Author:
Affiliation:
1. Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, Netherlands
2. Department of Radiation, Radionuclides and Reactors, Delft University of Technology, Mekelweg 15, 2629 JB, Delft, Netherlands
Abstract
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JB.00270-10
Reference33 articles.
1. Anderson, L. A., T. Palmer, N. C. Price, S. Bornemann, D. H. Boxer, and R. N. Pau. 1997. Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli. Eur. J. Biochem. 246 : 119-126.
2. Arendsen, A. F., P. T. M. Veenhuizen, and W. R. Hagen. 1995. Redox properties of the sulfhydrogenase from Pyrococcus furiosus. FEBS Lett. 368 : 117-121.
3. WOR5, a Novel Tungsten-Containing Aldehyde Oxidoreductase from Pyrococcus furiosus with a Broad Substrate Specificity
4. Tungsten Transport Protein A (WtpA) in Pyrococcus furiosus : the First Member of a New Class of Tungstate and Molybdate Transporters
5. Bevers, L. E., P. L. Hagedoorn, J. A. Santamaria-Araujo, A. Magalon, W. R. Hagen, and G. Schwarz. 2008. A function for MoaB in the biosynthesis of the molybdenum and tungsten cofactors. Biochemistry 47 : 949-956.
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