[NMR paper] Solution NMR characterization of magnetic/electronic properties of azide and cyanide-inhibited substrate complexes of human heme oxygenase: implications for steric ligand tilt.
Solution NMR characterization of magnetic/electronic properties of azide and cyanide-inhibited substrate complexes of human heme oxygenase: implications for steric ligand tilt.
Related ArticlesSolution NMR characterization of magnetic/electronic properties of azide and cyanide-inhibited substrate complexes of human heme oxygenase: implications for steric ligand tilt.
J Inorg Biochem. 2013 Apr;121:179-86
Authors: Peng D, Ogura H, Ma LH, Evans JP, de Montellano PR, La Mar GN
Abstract
Solution 2D (1)H NMR was carried out on the azide-ligated substrate complex of human heme oxygenase, hHO, to provide information on the active site molecular structure, chromophore electronic/magnetic properties, and the distal H-bond network linked to the exogenous ligand by catalytically relevant oriented water molecules. While 2D NMR exhibited very similar patterns of two-dimensional nuclear Overhauser spectroscopy cross peaks of residues with substrate and among residues as the previously characterized cyanide complex, significant, broadly distributed chemical shift differences were observed for both labile and non-labile protons. The anisotropy and orientation of the paramagnetic susceptibility tensor, ?, were determined for both the azide and cyanide complexes. The most significant difference observed is the tilt of the major magnetic axes from the heme normal, which is only half as large for the azide than cyanide ligand, with each ligand tilted toward the catalytically cleaved ?-meso position. The difference in chemical shifts is quantitatively correlated with differences in dipolar shifts in the respective complexes for all but the distal helix. The necessity of considering dipolar shifts, and hence determination of the orientation/anisotropy of ?, in comparing chemical shifts involving paramagnetic complexes, is emphasized. The analysis shows that the H-bond network cannot detect significant differences in H-bond acceptor properties of cyanide versus azide ligands. Lastly, significant retardation of distal helix labile proton exchange upon replacing cyanide with azide indicates that the dynamic stability of the distal helix is increased upon decreasing the steric interaction of the ligand with the distal helix.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Biochemistry. 2011 Aug 27;
Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN
Abstract
Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
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08-30-2011 04:52 PM
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
J Inorg Biochem. 2010 Oct;104(10):1063-70
Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN
Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
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02-10-2011 03:51 PM
[NMR paper] 13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of he
13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of heme proteins.
Related Articles 13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of heme proteins.
J Am Chem Soc. 2002 May 29;124(21):5936-7
Authors: Fujii H
13CN ion appears to have the greatest potential to probe the heme environment of the ferric heme proteins; however, a resonance of the iron-bound (13)CN ion in ferric heme proteins has not yet been located. We show here the first detection of (13)C NMR signals of the...
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11-24-2010 08:49 PM
[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 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] 2D NMR of paramagnetic metalloenzymes: cyanide-inhibited horseradish peroxidase.
2D NMR of paramagnetic metalloenzymes: cyanide-inhibited horseradish peroxidase.
Related Articles 2D NMR of paramagnetic metalloenzymes: cyanide-inhibited horseradish peroxidase.
J Biomol NMR. 1991 Jul;1(2):175-90
Authors: de Ropp JS, Yu LP, La Mar GN
Two-dimensional (2D) proton NMR correlation spectroscopy, COSY, and nuclear Overhauser spectroscopy, NOESY, have been used to explore the applicability of these methods for the moderately large (42 KDa), paramagnetic cyanide-inhibited derivative of horseradish peroxidase, HRP-CN. The target...
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08-21-2010 11:16 PM
[NMR paper] NMR study of the active site of resting state and cyanide-inhibited lignin peroxidase
NMR study of the active site of resting state and cyanide-inhibited lignin peroxidase from Phanerochaete chrysosporium. Comparison with horseradish peroxidase.
Related Articles NMR study of the active site of resting state and cyanide-inhibited lignin peroxidase from Phanerochaete chrysosporium. Comparison with horseradish peroxidase.
J Biol Chem. 1991 Aug 15;266(23):15001-8
Authors: de Ropp JS, La Mar GN, Wariishi H, Gold MH
One- and two-dimensional 1H NMR spectroscopy has been used to probe the active site of the high spin ferric resting...
Solution NMR characterization of magnetic/electronic properties of azide and cyanide-inhibited substrate complexes of human heme oxygenase: implications for steric ligand tilt.
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