| pubmed-article:12588121 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12588121 | lifeskim:mentions | umls-concept:C0040840 | lld:lifeskim |
| pubmed-article:12588121 | lifeskim:mentions | umls-concept:C0085481 | lld:lifeskim |
| pubmed-article:12588121 | lifeskim:mentions | umls-concept:C0302583 | lld:lifeskim |
| pubmed-article:12588121 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:12588121 | lifeskim:mentions | umls-concept:C1704332 | lld:lifeskim |
| pubmed-article:12588121 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:12588121 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:12588121 | lifeskim:mentions | umls-concept:C0916840 | lld:lifeskim |
| pubmed-article:12588121 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:12588121 | pubmed:dateCreated | 2003-2-17 | lld:pubmed |
| pubmed-article:12588121 | pubmed:abstractText | Superoxide reductases catalyze the monovalent reduction of superoxide anion to hydrogen peroxide. Spectroscopic evidence for the formation of a dinuclear cyano-bridged adduct after K(3)Fe(CN)(6) oxidation of the superoxide reductases neelaredoxin from Treponema pallidum and desulfoferrodoxin from Desulfovibrio vulgaris was reported. Oxidation with K(3)Fe(CN)(6) reveals a band in the near-IR with lambda(max) at 1020 nm, coupled with an increase of the iron content by almost 2-fold. Fourier transform infrared spectroscopy provided additional evidence with CN-stretching vibrations at 2095, 2025-2030, and 2047 cm(-)(1), assigned to a ferrocyanide adduct of the enzyme. Interestingly, the low-temperature electronic paramagnetic resonance (EPR) spectra of oxidized TpNlr reveal at least three different species indicating structural heterogeneity in the coordination environment of the active site Fe ion. Given the likely 6-coordinate geometry of the active site Fe(3+) ion in the ferrocyanide adduct, we propose that the rhombic EPR species can serve as a model of a hexacoordinate form of the active site. | lld:pubmed |
| pubmed-article:12588121 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12588121 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12588121 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12588121 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12588121 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12588121 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12588121 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12588121 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12588121 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12588121 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12588121 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12588121 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12588121 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12588121 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:12588121 | pubmed:issn | 0020-1669 | lld:pubmed |
| pubmed-article:12588121 | pubmed:author | pubmed-author:MouraIsabelI | lld:pubmed |
| pubmed-article:12588121 | pubmed:author | pubmed-author:MouraJosé J... | lld:pubmed |
| pubmed-article:12588121 | pubmed:author | pubmed-author:VenyaminovSer... | lld:pubmed |
| pubmed-article:12588121 | pubmed:author | pubmed-author:RusnakFrankF | lld:pubmed |
| pubmed-article:12588121 | pubmed:author | pubmed-author:AuchèreFranço... | lld:pubmed |
| pubmed-article:12588121 | pubmed:author | pubmed-author:TavaresPedroP | lld:pubmed |
| pubmed-article:12588121 | pubmed:author | pubmed-author:RaleirasPatrí... | lld:pubmed |
| pubmed-article:12588121 | pubmed:author | pubmed-author:BensonLindaL | lld:pubmed |
| pubmed-article:12588121 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12588121 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:12588121 | pubmed:volume | 42 | lld:pubmed |
| pubmed-article:12588121 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12588121 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12588121 | pubmed:pagination | 938-40 | lld:pubmed |
| pubmed-article:12588121 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12588121 | pubmed:meshHeading | pubmed-meshheading:12588121... | lld:pubmed |
| pubmed-article:12588121 | pubmed:meshHeading | pubmed-meshheading:12588121... | lld:pubmed |
| pubmed-article:12588121 | pubmed:meshHeading | pubmed-meshheading:12588121... | lld:pubmed |
| pubmed-article:12588121 | pubmed:meshHeading | pubmed-meshheading:12588121... | lld:pubmed |
| pubmed-article:12588121 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12588121 | pubmed:articleTitle | Formation of a stable cyano-bridged dinuclear iron cluster following oxidation of the superoxide reductases from Treponema pallidum and Desulfovibrio vulgaris with K(3)Fe(CN)(6). | lld:pubmed |
| pubmed-article:12588121 | pubmed:affiliation | Section of Hematology Research, Department of Biochemistry, Biomedical Mass Spectrometry Facility, Mayo Clinic, Rochester, Minnesota 55905, USA. | lld:pubmed |
| pubmed-article:12588121 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12588121 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12588121 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12588121 | lld:pubmed |
