| http://purl.uniprot.org/citations/16634620 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16634620 | http://www.w3.org/2000/01/rdf-schema#comment | "myo-Inositol oxygenase (MIOX) uses iron as its cofactor and dioxygen as its cosubstrate to effect the unique, ring-cleaving, four-electron oxidation of its cyclohexan-(1,2,3,4,5,6-hexa)-ol substrate to d-glucuronate. The nature of the iron cofactor and its interaction with the substrate, myo-inositol (MI), have been probed by electron paramagnetic resonance (EPR) and Mössbauer spectroscopies. The data demonstrate the formation of an antiferromagnetically coupled, high-spin diiron(III/III) cluster upon treatment of solutions of Fe(II) and MIOX with excess O(2) or H(2)O(2) and the formation of an antiferromagnetically coupled, valence-localized, high-spin diiron(II/III) cluster upon treatment with either limiting O(2) or excess O(2) in the presence of a mild reductant (e.g., ascorbate). Marked changes to the spectra of both redox forms upon addition of MI and analogy to changes induced by binding of phosphate to the diiron(II/III) cluster of the protein phosphatase, uteroferrin, suggest that MI coordinates directly to the diiron cluster, most likely in a bridging mode. The addition of MIOX to the growing family of non-heme diiron oxygenases expands the catalytic range of the family beyond the two-electron oxidation (hydroxylation and dehydrogenation) reactions catalyzed by its more extensively studied members such as methane monooxygenase and stearoyl acyl carrier protein Delta(9)-desaturase."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi0519607"xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/author | "Xing G."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/author | "Krebs C."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/author | "Bollinger J.M. Jr."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/author | "Prabhu K.S."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/author | "Reddy C.C."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/author | "Hoffart L.M."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/author | "Diao Y."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/author | "Arner R.J."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/pages | "5393-5401"xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/title | "A coupled dinuclear iron cluster that is perturbed by substrate binding in myo-inositol oxygenase."xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://purl.uniprot.org/core/volume | "45"xsd:string |
| http://purl.uniprot.org/citations/16634620 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16634620 |
| http://purl.uniprot.org/citations/16634620 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16634620 |
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