Related Articles1H NMR study of the solution molecular and electronic structure of Escherichia coli ferricytochrome b562: evidence for S = 1/2 in equilibrium S = 5/2 spin equilibrium for intact His/Met ligation.
Biochemistry. 1991 Feb 26;30(8):2156-65
Authors: Wu JZ, La Mar GN, Yu LP, Lee KB, Walker FA, Chiu ML, Sligar SG
The solution 500-MHz 1H NMR spectral parameters for ferricytochrome b562, a soluble 12-kDa electron carrier from Escherichia coli with axial His/Met coordination, are shown to be strongly influenced by protein concentration and ionic strength at low pH and 25 degrees C in a manner consistent with significant aggregation at low ionic strength. At high ionic strength a well-resolved 1H NMR spectrum reveals over 40 hyperfine-shifted resonances which arise from two isomeric species in the ratio 2:1. 2D COSY and NOESY maps at 25 degrees C for the hyperfine-shifted resonances allow the assignment of a number of axial His resonances and all heme peripheral substituent peaks. The resulting asymmetric heme contact shift patterns, together with the halving of the number of lines when reconstituting with 2-fold symmetric hemin, demonstrate the molecular basis of the solution heterogeneity to be heme orientational disorder. The strongly upfield-shifted axial Met-7 resonances, characteristic of low-spin ferricytochromes c with His/Met ligation, appear upfield only at very low temperatures. At elevated temperatures, all resonances, in particular those of the axial Met, move strongly downfield. Detailed analysis of the deviation from Curie behavior for different functional groups demonstrates the presence of a low spin in equilibrium high spin equilibrium with an intact His-Fe-Met coordination. The weaker axial field in ferricytochrome b562, relative to the purely low-spin ferricytochromes c, is attributed to a perturbed iron-Met bond. The contact shifts for a coordinated Met in the high-spin state are estimated. A link between equatorial hemin and axial ligand interactions is indicated by a differential population of the high-spin form for the two hemin orientations.
[NMR paper] Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli m
Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system.
Related Articles Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system.
J Biol Chem. 2005 May 27;280(21):20775-84
Authors: Williams DC, Cai M, Suh JY, Peterkofsky A, Clore GM
The solution structure of the 48-kDa IIA(Man)-HPr complex of the mannose branch of the Escherichia coli phosphotransferase system has been solved by NMR using conjoined rigid body/torsion...
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[NMR paper] Solution 1H NMR of the molecular and electronic structure of the heme cavity and subs
Solution 1H NMR of the molecular and electronic structure of the heme cavity and substrate binding pocket of high-spin ferric horseradish peroxidase: effect of His42Ala mutation.
Related Articles Solution 1H NMR of the molecular and electronic structure of the heme cavity and substrate binding pocket of high-spin ferric horseradish peroxidase: effect of His42Ala mutation.
J Am Chem Soc. 2001 May 9;123(18):4243-54
Authors: Asokan A, de Ropp JS, Newmyer SL, Ortiz de Montellano PR, La Mar GN
Solution 1H NMR has been used to assign a major portion...
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[NMR paper] Escherichia coli diacylglycerol kinase: a case study in the application of solution N
Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
Biophys J. 1997 Jun;72(6):2688-701
Authors: Vinogradova O,...
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[NMR paper] Escherichia coli diacylglycerol kinase: a case study in the application of solution N
Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
Biophys J. 1997 Jun;72(6):2688-701
Authors: Vinogradova O,...
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[NMR paper] Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli:
Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
Proc Natl Acad Sci U S A. 1994 May 24;91(11):5114-8
Authors: Newkirk K, Feng W, Jiang W, Tejero R, Emerson SD, Inouye M, Montelione GT
Sequence-specific...
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[NMR paper] NMR structure determination of the Escherichia coli DnaJ molecular chaperone: seconda
NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.
Proc Natl Acad Sci U S A. 1994 Nov...
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[NMR paper] 1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli
1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein.
Eur J Biochem. 1993 Aug 1;215(3):573-85
Authors: Bruix M, Pascual J, Santoro J, Prieto J, Serrano L, Rico M
Che Y is a 129-residue parallel alpha/beta protein involved in bacterial...
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[NMR paper] NMR study of the molecular and electronic structure of the heme cavity in Dolabella m
NMR study of the molecular and electronic structure of the heme cavity in Dolabella met-cyano myoglobin.
Related Articles NMR study of the molecular and electronic structure of the heme cavity in Dolabella met-cyano myoglobin.
Biochim Biophys Acta. 1993 Jun 4;1163(3):287-96
Authors: Yamamoto Y, Suzuki T
The molecular and electronic structure of the active site of the cyanide-ligated ferric complex of the myoglobin from the mollusc Dolabella auricularia has been investigated using NMR. Analysis of nuclear Overhauser effects has revealed that...