Doonan, C.Wilson, H.Bennett, B.Prince, R.Rajagopalan, K.George, G.2011-09-122011-09-122008Inorganic Chemistry: including bioinorganic chemistry, 2008; 47(6):2033-20380020-16691520-510Xhttp://hdl.handle.net/2440/66087Valuable 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.enCopyright 2008 American Chemical SocietyHumansChloridesMolybdenumElectron Spin Resonance SpectroscopyBinding SitesKineticsHydrogen-Ion ConcentrationThermodynamicsModels, MolecularSulfite OxidaseJournal article002011120910.1021/ic70170832-s2.0-4214911905228439