MoV Electron Paramagnetic Resonance of Sulfite Oxidase Revisited: The Low-pH Chloride Signal

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 MoV 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 ha...

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Veröffentlicht in:Inorganic chemistry 2008-03, Vol.47 (6), p.2033-2038
Hauptverfasser: Doonan, Christian J, Wilson, Heather L, Bennett, Brian, Prince, Roger C, Rajagopalan, K. V, George, Graham N
Format: Artikel
Sprache:eng
Schlagworte:
Binding Sites
Chlorides - chemistry
Electron Spin Resonance Spectroscopy - methods
Humans
Hydrogen-Ion Concentration
Kinetics
Models, Molecular
Molybdenum - chemistry
Sulfite Oxidase - chemistry
Sulfite Oxidase - metabolism
Thermodynamics
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Zusammenfassung:Valuable information on the active sites of molybdenum enzymes has been provided by MoV 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.
ISSN:0020-1669
1520-510X
DOI:10.1021/ic7017083