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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1991-3-21
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pubmed:abstractText |
Dipolar paramagnetic shifts for protons of yeast iso-1-cytochrome c have been calculated by using an optimized g-tensor and the X-ray crystallographic coordinates of the reduced form of yeast iso-1-cytochrome c [Louie, G. V., & Brayer, G. D. (1990) J. Mol. Biol. 214, 527-555]. The calculated values are compared with the observed paramagnetic shift determined from over 450 nonequivalent protons that have been assigned in both oxidation states [Gao, Y., Boyd, J., Williams, R. J. P., & Pielak, G. J. (1990) Biochemistry 29, 6994-7003]. There is good agreement between the calculated and the experimental data with a few exceptions. This indicates that, overall, the solution structures must be very similar in both the reduced and oxidized states in solution as is the case in crystals. The differences between observed and calculated shift values for the molecule in solution are most readily explained by slight movement of the heme and certain changes in diamagnetic shift due to small rearrangements of a few residues and some considerable changes in a few hydrogen bonds. It is also known that small differences exist between the structures of the two oxidation states in crystals but the hydrogen-bond changes are not so easily observed there. Structural changes from nuclear magnetic resonance data are in reasonable agreement with those deduced from crystallography, but additional information is clearly available concerning changes in hydrogen bonding.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CYC1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1928-34
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1847077-Animals,
pubmed-meshheading:1847077-Cytochrome c Group,
pubmed-meshheading:1847077-Cytochromes c,
pubmed-meshheading:1847077-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:1847077-Genetic Variation,
pubmed-meshheading:1847077-Kinetics,
pubmed-meshheading:1847077-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1847077-Oxidation-Reduction,
pubmed-meshheading:1847077-Protein Conformation,
pubmed-meshheading:1847077-Protons,
pubmed-meshheading:1847077-Saccharomyces cerevisiae,
pubmed-meshheading:1847077-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:1847077-X-Ray Diffraction
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pubmed:year |
1991
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pubmed:articleTitle |
Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts.
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pubmed:affiliation |
Inorganic Chemistry Laboratory, University of Oxford, U.K.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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