Related Articles1H-NMR and EPR studies on met-azido and met-imidazole Dolabella auricularia myoglobin.
Biochim Biophys Acta. 1995 Apr 27;1248(2):149-58
Authors: Yamamoto Y, Suzuki T, Hori H
Met-azido and met-imidazole forms of the myoglobin from the mollusc Dolabella auricularia have been studied by 1H-NMR and EPR spectroscopy. In the mollusc myoglobin, in which His-E7 is replaced by Val, the guanidino group of Arg-E10 serves as an alternative hydrogen-bond donor to the bound ligand. Therefore, the guanidino group of Arg-E10 plays similar roles in ligand stabilization to that the His-E7 imidazole does in most vertebrate myoglobins. Differences in both the structural and electronic properties between Arg and His side chains largely affect the stability of met-azido and met-imidazole forms of the protein. Due to a weak stabilization by Arg-E10, the bound-N3- ligand is replaced by OH- at higher pH, although it is stable at neutral and acidic pH. In the absence of the hydrogen-bonding interaction, Fe-bound imidazole in met-imidazole Dolabella myoglobin is only stable at neutral pH and is removed at acidic pH and replaced by OH- at basic pH. The temperature study also revealed that the bound imidazole is replaced by OH- at higher temperature. These results confirm that the presence of steric hindrance between these bulky ligands and the long and bulky side chain of Arg-E10 in the distal pocket of the mollusc myoglobin. Thus steric effects contribute significantly to the stability of exogenous ligand in the distal pocket of myoglobin.
[NMR paper] Identification of regioisomers in a series of N-substituted pyridin-4-yl imidazole de
Identification of regioisomers in a series of N-substituted pyridin-4-yl imidazole derivatives by regiospecific synthesis, GC/MS, and 1H NMR.
Related Articles Identification of regioisomers in a series of N-substituted pyridin-4-yl imidazole derivatives by regiospecific synthesis, GC/MS, and 1H NMR.
J Org Chem. 2003 May 30;68(11):4527-30
Authors: Wagner GK, Kotschenreuther D, Zimmermann W, Laufer SA
The regiospecific synthesis of 2a (Scheme 3), a novel and potent pyridinyl imidazole inhibitor of p38 MAP (mitogen-activated protein) kinase, and...
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[NMR paper] 1H NMR structure of the heme pocket of HNO-myoglobin.
1H NMR structure of the heme pocket of HNO-myoglobin.
Related Articles 1H NMR structure of the heme pocket of HNO-myoglobin.
J Biol Inorg Chem. 2003 Feb;8(3):348-52
Authors: Sulc F, Fleischer E, Farmer PJ, Ma D, La Mar GN
The unique (1)H NMR signal of nitrosyl hydride at 14.8 ppm is used to obtain a solution structure of the distal pocket of Mb-HNO, a rare nitroxyl adduct with a half-life of several months at room temperature. (1)H NMR, NOESY and TOCSY data were obtained under identical experimental conditions on solutions of the diamagnetic...
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[NMR paper] 1H-NMR measurement of fractional dissociation of imidazole in intact animals.
1H-NMR measurement of fractional dissociation of imidazole in intact animals.
Related Articles 1H-NMR measurement of fractional dissociation of imidazole in intact animals.
Am J Physiol. 1994 Mar;266(3 Pt 2):R1008-15
Authors: Hitzig BM, Perng WC, Burt T, Okunieff P, Johnson DC
The alphastat hypothesis states that intracellular acid-base status is regulated to maintain constancy of the fractional dissociation of intracellular protein and enzyme imidazole-histidine (alpha-imidazole). A major drawback of this theory has been the lack of a means...
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[NMR paper] 1H-NMR measurement of fractional dissociation of imidazole in intact animals.
1H-NMR measurement of fractional dissociation of imidazole in intact animals.
Related Articles 1H-NMR measurement of fractional dissociation of imidazole in intact animals.
Am J Physiol. 1994 Mar;266(3 Pt 2):R1008-15
Authors: Hitzig BM, Perng WC, Burt T, Okunieff P, Johnson DC
The alphastat hypothesis states that intracellular acid-base status is regulated to maintain constancy of the fractional dissociation of intracellular protein and enzyme imidazole-histidine (alpha-imidazole). A major drawback of this theory has been the lack of a means...
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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...
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[NMR paper] Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellu
Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellular oxygenation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellular oxygenation.
Proc Natl Acad Sci U S A. 1992 May 15;89(10):4731-3
Authors: Kreutzer U, Wang DS, Jue T
The 1H NMR signal from oxymyoglobin, a low-concentration diamagnetic protein, is visible in myocardial tissue. The methyl...
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[NMR paper] NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural altera
NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural alteration on the active site of G. japonicus myoglobin upon azide ion binding.
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 NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural alteration on the active site of G. japonicus myoglobin upon azide ion binding.
Eur J Biochem. 1991 Jun 1;198(2):285-91
Authors: Yamamoto Y, Chûjô R, Suzuki T...
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(2)H NMR study of the water dynamics in hydrated myoglobin.
(2)H NMR study of the water dynamics in hydrated myoglobin.
Related Articles (2)H NMR study of the water dynamics in hydrated myoglobin.
J Phys Chem B. 2010 Aug 12;114(31):10209-16
Authors: Lusceac SA, Vogel M
We use 1D and 2D (2)H NMR to study the temperature-dependent mechanism for the rotational motion of myoglobin hydration water. The results show that isotropic and anisotropic water reorientation is observed at high and low temperatures, respectively, with a continuous crossover in the temperature range of 200-230 K. The anisotropic...
1H-NMR and EPR studies on met-azido and met-imidazole Dolabella auricularia myoglobin
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