Source:http://linkedlifedata.com/resource/pubmed/id/11890810
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
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| pubmed:dateCreated |
2002-3-13
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| pubmed:abstractText |
Despite the current availability of several crystal structures of purple acid phosphatases, to date there is no direct evidence for solvent-derived ligands occupying terminal positions in the active enzyme. This is of central importance, because catalysis has been shown to proceed through the direct attack on a metal-bound phosphate ester by a metal-activated solvent-derived moiety, which has been proposed to be either (i) a hydroxide ligand terminally bound to the ferric center or (ii) a bridging hydroxide. In this work we use (2)H Q-band (35 GHz) pulsed electron-nuclear double resonance (ENDOR) spectroscopy to identify solvent molecules coordinated to the active mixed-valence (Fe(3+)Fe(2+)) form of the dimetal center of uteroferrin (Uf), as well as to its complexes with the anions MoO(4), AsO(4), and PO(4). The solvent-derived coordination of the dinuclear center of Uf as deduced from ENDOR data includes a bridging hydroxide and a terminal water/hydroxide bound to Fe(2+) but no terminal water/hydroxide bound to Fe(3+). The terminal water is lost upon anion binding while the hydroxyl bridge remains. These results are not compatible with a hydrolysis mechanism involving a terminal Fe(3+)-bound nucleophile, but they are consistent with a mechanism that relies on the bridging hydroxide as the nucleophile.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acid Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Arsenates,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molybdenum,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Solvents,
http://linkedlifedata.com/resource/pubmed/chemical/Water,
http://linkedlifedata.com/resource/pubmed/chemical/arsenic acid,
http://linkedlifedata.com/resource/pubmed/chemical/molybdate,
http://linkedlifedata.com/resource/pubmed/chemical/tartrate-resistant acid phosphatase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
0002-7863
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
20
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| pubmed:volume |
124
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2595-603
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:11890810-Acid Phosphatase,
pubmed-meshheading:11890810-Arsenates,
pubmed-meshheading:11890810-Binding Sites,
pubmed-meshheading:11890810-Catalysis,
pubmed-meshheading:11890810-Hydrolases,
pubmed-meshheading:11890810-Iron,
pubmed-meshheading:11890810-Isoenzymes,
pubmed-meshheading:11890810-Metalloproteins,
pubmed-meshheading:11890810-Molybdenum,
pubmed-meshheading:11890810-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:11890810-Phosphates,
pubmed-meshheading:11890810-Solvents,
pubmed-meshheading:11890810-Water
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| pubmed:year |
2002
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| pubmed:articleTitle |
Electro-nuclear double resonance spectroscopic evidence for a hydroxo-bridge nucleophile involved in catalysis by a dinuclear hydrolase.
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| pubmed:affiliation |
Department of Chemistry, Northwestern University, Evanston, Illinois 60208, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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