Linked Life Data

21190336

Source:http://linkedlifedata.com/resource/pubmed/id/21190336

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-1-31
pubmed:abstractText
We report a structural characterization using X-ray absorption spectroscopy of the molybdenum site of Escherichia coli YedY, a novel oxidoreductase related to be the sulfite oxidase family of molybdenum enzymes. We find that the enzyme can exist in Mo(V) and Mo(IV) oxidation states but cannot be readily oxidized to the Mo(VI) form. Mo(V) YedY has molybdenum coordination similar to that of sulfite oxidase, with one Mo?O at 1.71 Å, three Mo-S at 2.39 Å, and one Mo-OH at 2.09 Å, which elongates to 2.20 Å upon reduction to Mo(IV), indicating Mo-OH(2) coordination. The Mo(V) enzyme also possesses a long Mo-O coordination at 2.64 Å, which may be due to oxygen coordination by Asn-45 O(?), with Mo-O(?) approximately trans to the Mo?O group. A comparison with sulfite oxidase indicates that YedY possesses a much more uniform Mo-S coordination, with a maximum permitted deviation of less than 0.05 Å. Our results indicate that the YedY active site shows considerable similarity to but also important differences from that of reduced forms of sulfite oxidase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1520-510X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
7
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
732-40
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Molybdenum site structure of Escherichia coli YedY, a novel bacterial oxidoreductase.
pubmed:affiliation
Department of Geological Sciences, University of Saskatchewan, Saskatoon, Saskatchewan, Canada.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural