Linked Life Data

18399627

Source:http://linkedlifedata.com/resource/pubmed/id/18399627

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2008-4-29
pubmed:abstractText
In view of the biological and commercial interest in models for Oxalate Decarboxylases (OxDC) and Oxalate Oxidases (OxOx), we have synthesized and characterized three new Mn (II) complexes ( 1- 3) employing N3O-donor amino-carboxylate ligands (TCMA, 1,4,7-triazacyclononane- N-acetic acid; K (i) Pr 2TCMA, potassium 1,4-diisopropyl-1,4,7-triazacyclononane- N-acetate; and KBPZG, potassium N,N-bis(3,5-dimethylpyrazolyl methyl)glycinate). These complexes were characterized by several techniques including X-ray crystallographic analysis, X-band electron paramagnetic resonance (EPR), electrospray ionization mass spectrometry (ESI-MS), and cyclic voltammetry. The crystal structures of 1 and 3 revealed that both form infinite polymeric chains of Mn (II) complexes linked by the pendant carboxylate arms of the TCMA (-) and the BPZG (-) ligands in a syn-antipattern. Complex 2 crystallizes as a mononuclear Mn (II) cation, six-coordinate in a distorted octahedral geometry. Although complexes 1 and 3 crystallize as polymeric chains, all compounds present the same N3O-donor set atoms around the metal center as observed in the crystallographically characterized OxDC and OxOx. Moreover, complex 2 also contains two water molecules coordinated to the Mn center as observed in the active site of OxDC and OxOx. ESI-MS spectrometry, combined with EPR, were useful techniques to establish that complexes 1- 3 are present as mononuclear Mn (II) species in solution. Finally, complexes 1- 3 are able to model the resting state active sites, with special attention focused on complex 2 which provides the first exact first coordination sphere ligand structural model for the resting states of both OxDC and OxOx.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0020-1669
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3584-93
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Modeling the resting state of oxalate oxidase and oxalate decarboxylase enzymes.
pubmed:affiliation
Willard H. Dow Laboratories, Department of Chemistry, University of Michigan, 930 North University, Ann Arbor, MI 48109, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural