MoV electron paramagnetic resonance of sulfite oxidase revisited: the low-pH chloride signal.
Valuable information on the active sites of molybdenum enzymes has been provided by Mo(V) electron paramagnetic resonance (EPR) spectroscopy. In recent years, multiple resonance techniques have been extensively used to examine details of the active-site structure, but basic continuous-wave (CW) EPR has not been re-evaluated in several decades. Here, we present a re-examination of the CW EPR spectroscopy of the sulfite oxidase low-pH chloride species and provide evidence for direct coordination of molybdenum by chloride.
Doonan
Christian J
CJ
Department of Geological Sciences, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E2, Canada.
Wilson
Heather L
HL
Bennett
Brian
B
Prince
Roger C
RC
Rajagopalan
K V
KV
George
Graham N
GN
D001665:Binding Sites; D002712:Chlorides / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008958:Models, Molecular; D008982:Molybdenum / Q000737:chemistry; D050876:Sulfite Oxidase / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics
D002712:Chlorides; D008982:Molybdenum; D050876:Sulfite Oxidase