Linked Life Data

14599210

Source:http://linkedlifedata.com/resource/pubmed/id/14599210

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
45
pubmed:dateCreated
2003-11-5
pubmed:abstractText
In agreement with previous reports (Gasyna, Z. FEBS Lett. 1979, 106, 213-218 and Leibl, W.; Nitschke, W.; Huettermann, J. Biochim. Biophys. Acta 1986, 870, 20-30) radiolytically reduced samples of oxygenated myoglobin at cryogenic temperatures have been shown by optical absorption and EPR studies to produce directly the peroxo-bound myoglobin at 77 K. Annealing to temperatures near 185 K induces proton transfer, resulting in the formation of the hydroperoxo heme derivative. Resonance Raman studies of the annealed samples has permitted, for the first time, the direct observation of the key nu(Fe-O) stretching mode of the physiologically important Fe-OOH fragment of this ubiquitous intermediate. The assignment of this mode to a feature appearing at 617 cm(-1) is strongly supported by documentation of a 25 cm(-1) shift to lower energy upon substitution with (18)O(2) and by a 5 cm(-1) shift to lower energy for samples prepared in solutions of deuterated solvent.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13714-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Resonance Raman spectroscopic studies of hydroperoxo-myoglobin at cryogenic temperatures.
pubmed:affiliation
Department of Chemistry, Marquette University, Milwaukee, Wisconsin 53233, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't