Linked Life Data

7068674

Source:http://linkedlifedata.com/resource/pubmed/id/7068674

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1982-6-24
pubmed:abstractText
We report the observation of deuterium Fourier transform NMR spectra (obtained by the quadrupole echo method at 8.5 Tesla, corresponding to a 2H resonance frequency of 55.3 MHz) of [meso-alpha, beta, gamma, delta-2H4], [methyl-1,3-2H6], and [methylene-6,7-b-2H4]heme-labeled aquoferrimyoglobin microcrystals (in approximately 90% saturated (NH4)2SO4 at pH 6.8) from Physeter catodon, using the method of magnetic ordering (Rothgeb, T. M. and Oldfield, E. (1981) J. Biol. Chem. 256, 1432-1446). The results, together with those obtained on suitable diamagnetic derivatives, permit partial determination of the static organization of the heme, and the results obtained are in good agreement with those obtained using x-ray crystallography (Takano, T. (1977( J. Mol. Biol. 110, 537-568). We show that resonances near the paramagnetic iron center are subject to extremely large (approximately 500 ppm) hyperfine shifts, which distort the otherwise symmetric 2H spectra. Temperature dependence studies are required to analyze these shifts, which are an order of magnitude larger than those seen in solution NMR spectroscopy. The overall results suggest that 2H solid state NMR spectroscopy of magnetically ordered paramagnetic protein microcrystals may be a useful method for determination of heme organization in systems that for one reason or another are unsuitable for analysis using x-ray diffraction methods.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5023-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Nuclear magnetic resonance of hemeprotein crystals. Structure of the heme in Physeter catodon ferrimyoglobin and an analysis of hyperfine shifts.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't