Related ArticlesProton NMR study of the heme complex of hemopexin.
Biochim Biophys Acta. 1994 Jul 6;1200(2):161-6
Authors: Deeb RS, Muller-Eberhard U, Peyton DH
Proton nuclear magnetic resonance spectroscopy of the complex of heme with hemopexin, a plasma protein with an exceptionally high affinity for heme, is reported. Characteristic spectra are shown for heme.hemopexin of cow, human, rabbit, and rat. Each of these spectra demonstrate that the iron of heme bound by hemopexin is paramagnetic and low-spin. Rabbit heme.hemopexin, which exhibits the best signal-to-noise ratio, is studied in detail. Deuterium isotope labeling experiments indicate that the methyls in heme positions 1-, 3-, and 8- are resolved downfield from the protein envelope of resonances; the 5-methyl may lie in the -5 to +12 ppm region. Two-dimensional nuclear Overhauser effect spectroscopy locates other protons of the heme periphery, including from the 2-vinyl. Strongly relaxed upfield resonances are identified and assigned to protons on the axial ligands. Cyanide interaction with heme.hemopexin produces an additional low-spin adduct.
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] Proton NMR study of the heme environment in bacterial quinol oxidases.
Proton NMR study of the heme environment in bacterial quinol oxidases.
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Arch Biochem Biophys. 2004 Jan 15;421(2):186-91
Authors: Zhang J, Osborne JP, Gennis RB, Wang X
The heme environment and ligand binding properties of two relatively large membrane proteins containing multiple paramagnetic metal centers, cytochrome bo3 and bd quinol oxidases, have been studied by high field proton nuclear magnetic resonance (NMR) spectroscopy. The oxidized bo3 enzyme...
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[NMR paper] Proton NMR investigation of the heme active site structure of an engineered cytochrom
Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Related Articles Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Biochemistry. 1999 Jul 13;38(28):9146-57
Authors: Wang X, Lu Y
The heme active site structure of an engineered cytochrome c peroxidase that closely mimics manganese peroxidase (MnP) has been characterized by both one- and two-dimensional NMR spectroscopy. All...
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11-18-2010 08:31 PM
[NMR paper] MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domai
MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain.
Related Articles MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain.
Biochim Biophys Acta. 1995 Dec 6;1253(2):215-23
Authors: Cox MC, Le Brun N, Thomson AJ, Smith A, Morgan WT, Moore GR
Heme binding to rabbit hemopexin and its domain I, obtained by proteolytic cleavage of intact hemopexin, was studied by EPR, MCD and 1H-NMR spectroscopies. The data obtained support the proposal that the heme Fe(III) is coordinated by two...
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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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08-22-2010 03:33 AM
[NMR paper] Proton NMR assignments of heme contacts and catalytically implicated amino acids in c
Proton NMR assignments of heme contacts and catalytically implicated amino acids in cyanide-ligated cytochrome c peroxidase determined from one- and two-dimensional nuclear Overhauser effects.
Related Articles Proton NMR assignments of heme contacts and catalytically implicated amino acids in cyanide-ligated cytochrome c peroxidase determined from one- and two-dimensional nuclear Overhauser effects.
Biochemistry. 1991 May 7;30(18):4398-405
Authors: Satterlee JD, Erman JE
Proton NMR assignments of the heme pocket and catalytically relevant...
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[NMR paper] 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket st
1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5.
Related Articles 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5.
Biochemistry. 1991 Feb 19;30(7):1878-87
Authors: Lee KB, La Mar GN, Pandey RK, Rezzano IN, Mansfield KE, Smith KM
1H nuclear magnetic resonance spectroscopy was used to assign the hyperfine-shifted resonances and determine the position of...
Proton NMR study of the heme complex of hemopexin.
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