Related ArticlesProton NMR study of the comparative electronic/magnetic properties and dynamics of the acid in equilibrium with alkaline transition in a series of ferricytochromes c'.
J Biol Chem. 1990 Sep 25;265(27):16173-80
Authors: La Mar GN, Jackson JT, Dugad LB, Cusanovich MA, Bartsch RG
The proton NMR spectra of ferricytochrome c' from Rhodopseudomonas palustris, Rhodospirillum molischianum, Rhodospirillum rubrum, and Chromatium vinosum have been investigated for the purpose of further elucidating the common spectral and/or structural properties for this subclass of cytochromes in the acidic and alkaline forms, and to characterize in detail the dynamics and structural basis for this acid in equilibrium with alkaline transition. The identification of strongly upfield-shifted meso-H peaks in all but C. vinosum ferricytochrome c' at weakly acidic to neutral pH is consistent with, but not proof for, S = 3/2 character for the spin state of C. vinosum, but argues for primarily S = 5/2 character for the other three proteins. Hence, we conclude that the quantum mechanically mixed S = 3/2, S = 5/2 spin ground state of neutral pH C. vinosum ferricytochrome c' is an anomaly rather than a characteristic of this class of proteins. The 1H NMR spectra of ferricytochromes c' at alkaline pH again exhibit strong similarities among all members except that for C. vinosum. Two pK values are observed for ferricytochrome c' for R. molischianum and C. vinosum, of which the higher value pK is accompanied by significant line broadening, as found earlier for the proteins from both R. rubrum and R. palustris. Detailed analysis of the exchange line broadening for all four proteins reveals that hydrolysis is the rate-limiting step, with base catalysis occurring at about the same rate in the diffusion control limit for all four proteins. The variable first order dissociation rates of the alkaline species reveal differential stabilities of that species in the order R. palustris greater than R. molischianum greater than R. rubrum much greater than C. vinosum. The rates of exchange of the axial His imidazole labile proton was determined by linewidth and saturation transfer analysis and shown to occur via base catalysis at the same diffusion control rate as found for the acid----alkaline transition for the oxidized protein, and support the proposal that the acid----alkaline transition involves simply the abstraction of a proton from the neutral His imidazole to yield an imidazolate.
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Biochim Biophys Acta. 2011 May 6;
Authors: Juillard S, Chevance S, Bondon A, Simonneaux G
The asymmetric 3-ethyl-2-methylporphyrin iron complex was synthetized and inserted into apomyoglobin. UV-visible spectroscopic studies demonstrated the capacity of iron to coordinate different exogenous axial ligands in ferrous and...
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[NMR paper] Solution 1H NMR study of the active site molecular structure and magnetic properties
Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin.
Related Articles Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin.
Biochim Biophys Acta. 2004 Sep 1;1701(1-2):75-87
Authors: Tran AT, Kolczak U, La Mar GN
The solution molecular structure and the electronic and magnetic properties of the heme...
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[NMR paper] 19F NMR study of protein-induced rhombic perturbations on the electronic structure of
19F NMR study of protein-induced rhombic perturbations on the electronic structure of the active site of myoglobin.
Related Articles 19F NMR study of protein-induced rhombic perturbations on the electronic structure of the active site of myoglobin.
J Biol Inorg Chem. 2000 Aug;5(4):455-62
Authors: Yamamoto Y, Hirai Y, Suzuki A
A novel C2-symmetric ring-fluorinated hemin, 13,17-bis(2-carboxyethyl)-2,8,12,18-tetramethyl-3,7-difluoroporphyrin atoiron(III), has been synthesized and was incorporated into sperm whale apomyoglobin to investigate...
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[NMR paper] Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic a
Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Related Articles Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Biochemistry. 1994 May 31;33(21):6631-41
Authors: Hernández G, Wilks A, Paolesse R, Smith KM, Ortiz de Montellano PR, La Mar GN
The substrate-bound form of the enzyme heme oxygenase (HO), which catalyzed the stereospecific alpha-meso bridge...
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[NMR paper] Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic a
Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Related Articles Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Biochemistry. 1994 May 31;33(21):6631-41
Authors: Hernández G, Wilks A, Paolesse R, Smith KM, Ortiz de Montellano PR, La Mar GN
The substrate-bound form of the enzyme heme oxygenase (HO), which catalyzed the stereospecific alpha-meso bridge...
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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] 1H NMR study of the solution molecular and electronic structure of Escherichia coli f
1H 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.
Related Articles 1H 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...
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[NMR paper] Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the
Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
Related Articles Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
Biochemistry. 1990 Sep 18;29(37):8797-804
Authors: Satterlee JD, Erman JE, Mauro JM, Kraut J
Proton NMR spectra of cytochrome c peroxidase (CcP) isolated from yeast (wild type) and two Escherichia coli...