Related Articles1H 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 HNO and CO complexes of equine Mb, allowing direct comparison of NMR data to a crystallographically characterized structure. Twenty NOEs between the nitrosyl hydride and protein and heme-based signals were observed. The HNO orientation obtained by modeling the experimental (1)H NMR NOESY data yielded an orientation of ca. -104 degrees referenced to the N-Fe-N vector between alpha and beta mesoprotons. An essentially identical orientation was obtained by simple energy minimization of the HNO adduct using ESFF potentials, suggesting steric control of the orientation. Differences in chemical shifts are seen for protons on residues Phe43(CD1) and Val68(E11), but both exhibit virtually identical NOESY contacts to other residues, and thus are attributed to small movements of ca. 0.1 A within the strong ring current. The most significant differences are seen in the NOESY peak intensities and chemical shifts for the ring non-labile protons of the distal His64(E7). The orientation of the His64(E7) in Mb-HNO was analyzed on the basis of the NOESY cross-peak changes and chemical shift changes, predicting a ca. 20 degrees rotation about the beta-gamma bond. The deduced HNO and His64(E7) orientations result in geometry where the His64(E7) ring can serve as the donor for a significant H-bond to the oxygen atom of the bound HNO.
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] NMR structure of the thromboxane A2 receptor ligand recognition pocket.
NMR structure of the thromboxane A2 receptor ligand recognition pocket.
Related Articles NMR structure of the thromboxane A2 receptor ligand recognition pocket.
Eur J Biochem. 2004 Jul;271(14):3006-16
Authors: Ruan KH, Wu J, So SP, Jenkins LA, Ruan CH
To overcome the difficulty of characterizing the structures of the extracellular loops (eLPs) of G protein-coupled receptors (GPCRs) other than rhodopsin, we have explored a strategy to generate a three-dimensional structural model for a GPCR, the thromboxane A(2) receptor. This three-dimensional...
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[NMR paper] Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
Related Articles Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
J Biol Chem. 2003 Mar 7;278(10):7765-74
Authors: Wang X, Tachikawa H, Yi X, Manoj KM, Hager LP
The heme active site structure of chloroperoxidase (CPO), a glycoprotein that displays versatile catalytic activities isolated from the marine mold Caldariomyces fumago, has been characterized by two-dimensional NMR spectroscopic studies. All hyperfine shifted resonances...
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[NMR paper] Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
Related Articles Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
Biochemistry. 1994 Sep 13;33(36):10934-43
Authors: Busse SC, Jue T
Traditionally, assigning the heme protein resonances has relied heavily on the comparison of spectra arising from protein reconstituted with specifically deuterated hemes and the native form. Such an approach can identify tentatively the broad, overlapping signals in the Fe(II) high-spin heme protein spectra. Although...
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[NMR paper] 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
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-NMR study of reduced heme proteins myoglobin and cytochrome P450.
Eur J Biochem. 1993 Jul 15;215(2):431-7
Authors: Banci L, Bertini I, Marconi S, Pierattelli R
The 1H-NMR spectra of deoxymyoglobin and reduced cytochrome P450 are analyzed by NOE spectroscopy. Progress has been made in the assignment of the...
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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...
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[NMR paper] Characterization by NMR of the heme-myoglobin adduct formed during the reductive meta
Characterization by NMR of the heme-myoglobin adduct formed during the reductive metabolism of BrCCl3. Covalent bonding of the proximal histidine to the ring I vinyl group.
Related Articles Characterization by NMR of the heme-myoglobin adduct formed during the reductive metabolism of BrCCl3. Covalent bonding of the proximal histidine to the ring I vinyl group.
J Biol Chem. 1991 Feb 15;266(5):3208-14
Authors: Osawa Y, Highet RJ, Bax A, Pohl LR
The reductive debromination of BrCCl3 by ferrous deoxymyoglobin leads to the covalent bonding of the...
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[NMR paper] 1H-NMR study of heme propanoate mobility in the active site of myoglobin from Galeorh
1H-NMR study of heme propanoate mobility in the active site of myoglobin from Galeorhinus japonicus.
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-NMR study of heme propanoate mobility in the active site of myoglobin from Galeorhinus japonicus.
Eur J Biochem. 1990 May 20;189(3):567-73
Authors: Yamamoto Y, Inoue Y, Chûjô R, Suzuki T
Time-dependent NOE studies of the C13(1) and C17(1) methylene proton resonances of the heme...