MoV electron paramagnetic resonance of sulfite oxidase revisited: the low-pH chloride signal

dc.contributor.authorDoonan, C.
dc.contributor.authorWilson, H.
dc.contributor.authorBennett, B.
dc.contributor.authorPrince, R.
dc.contributor.authorRajagopalan, K.
dc.contributor.authorGeorge, G.
dc.date.issued2008
dc.description.abstractValuable 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.
dc.description.statementofresponsibilityChristian J. Doonan, Heather L. Wilson, Brian Bennett, Roger C. Prince, K. V. Rajagopalan, and Graham N. George
dc.identifier.citationInorganic Chemistry: including bioinorganic chemistry, 2008; 47(6):2033-2038
dc.identifier.doi10.1021/ic7017083
dc.identifier.issn0020-1669
dc.identifier.issn1520-510X
dc.identifier.urihttp://hdl.handle.net/2440/66087
dc.language.isoen
dc.publisherAmer Chemical Soc
dc.rightsCopyright 2008 American Chemical Society
dc.source.urihttps://doi.org/10.1021/ic7017083
dc.subjectHumans
dc.subjectChlorides
dc.subjectMolybdenum
dc.subjectElectron Spin Resonance Spectroscopy
dc.subjectBinding Sites
dc.subjectKinetics
dc.subjectHydrogen-Ion Concentration
dc.subjectThermodynamics
dc.subjectModels, Molecular
dc.subjectSulfite Oxidase
dc.titleMoV electron paramagnetic resonance of sulfite oxidase revisited: the low-pH chloride signal
dc.typeJournal article
pubs.publication-statusPublished

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