One- and two-electron reduction of molybdate reversibly bound to the archaeal tungstate/molybdate transporter WtpA.
Reversible binding of the tetrahedral oxoanions MoO(4)(2-) and WO(4)(2-) to two carboxylato ligands of the soluble scavenger protein WtpA from the hyperthermophilic archaeon Pyrococcus furiosus enforces a quasi-octahedral MO(6) coordination in which the +VI oxidation state is destabilized.
Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC, Delft, The Netherlands.
Loes E
LE
Bevers
Wilfred R
WR
Hagen
D019843:Archaeal Proteins / Q000378:metabolism*; D004583:Electrons; D008982:Molybdenum / Q000737:chemistry*; D010084:Oxidation-Reduction; D020027:Pyrococcus furiosus / Q000201:enzymology; D017973:Tungsten Compounds / Q000737:chemistry*
D019843:Archaeal Proteins; D017973:Tungsten Compounds; C044659:molybdate; D008982:Molybdenum; C045951:tungstate