Linked Life Data

2548601

Source:http://linkedlifedata.com/resource/pubmed/id/2548601

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1989-10-6
pubmed:abstractText
The active site of sulfite oxidase has been investigated by X-ray absorption spectroscopy at the molybdenum K-edge at 4 K. We have investigated all three accessible molybdenum oxidation states, Mo(IV), Mo(V), and Mo(VI), allowing comparison with the Mo(V) electron paramagnetic resonance data for the first time. Quantitative analysis of the extended X-ray absorption fine structure indicates that the Mo(VI) oxidation state possesses two terminal oxo (Mo = O) and approximately three thiolate-like (Mo-S-) ligands and is unaffected by changes in pH and chloride concentration. The Mo(IV) and Mo(V) oxidation states, however, each have a single oxo ligand plus one Mo-O- (or Mo-N less than) bond, most probably Mo--OH, and two to three thiolate-like ligands. Both reduced forms appear to gain a single chloride ligand under conditions of low pH and high chloride concentration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5075-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Structure of the active site of sulfite oxidase. X-ray absorption spectroscopy of the Mo(IV), Mo(V), and Mo(VI) oxidation states.
pubmed:affiliation
Exxon Research and Engineering Company, Annandale, New Jersey 08801.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.