Pyrococcus furiosusglyceraldehyde 3-phosphate oxidoreductase has comparable W6+/5+and W5+/4+reduction potentials and unusual [4Fe-4S] EPR properties
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(99)01511-2/fullpdf
Reference24 articles.
1. Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase
2. Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 Å resolution crystal structure and its mechanistic implications 1 1Edited by I. A. Wilson
3. Spectroscopic Characterization of the Tungsten and Iron Centers in Aldehyde Ferredoxin Oxidoreductases from Two Hyperthermophilic Archaea
4. Glyceraldehyde-3-phosphate Ferredoxin Oxidoreductase, a Novel Tungsten-containing Enzyme with a Potential Glycolytic Role in the Hyperthermophilic Archaeon Pyrococcus furiosus
5. Purification and Molecular Characterization of the Tungsten-Containing Formaldehyde Ferredoxin Oxidoreductase from the Hyperthermophilic Archaeon Pyrococcus furiosus : the Third of a Putative Five-Member Tungstoenzyme Family
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