Related Articles1H-NMR comparative study of the active site in shark (Galeorhinus japonicus), horse, and sperm whale deoxy myoglobins.
J Biochem. 1992 Sep;112(3):414-20
Authors: Yamamoto Y, Iwafune K, Chûjô R, Inoue Y, Imai K, Suzuki T
1H-NMR spectra of deoxy myoglobins (Mbs) from shark (Galeorhinus japonicus), horse, and sperm whale have been studied to gain insights into their active site structure. It has been demonstrated for the first time that nuclear Overhauser effect (NOE) can be observed between heme peripheral side-chain proton resonances of these paramagnetic complexes. Val-E11 methyl and His-F8 C delta H proton resonances of these Mbs were also assigned from the characteristic shift and line width. The hyperfine shift of the former resonance was used to calculate the magnetic anisotropy of the protein. The shift analysis of the latter resonance, together with the previously assigned His-F8 N delta H proton resonance, revealed that the strain on the Fe-N epsilon bond is in the order horse Mb approximately whale Mb < shark Mb and that the hydrogen bond strength of the His-F8 N delta H proton to the main-chain carbonyl oxygen in the preceding turn of the F helix is in the order shark Mb < horse Mb < whale Mb. Weaker Feporphyrin interaction in shark Mb was manifested in a smaller shift of the heme methyl proton resonance and appears to result from distortion of the coordination geometry in this Mb. Larger strain on the Fe-N epsilon bond in shark Mb should be to some extent attributed to its lowered O2 affinity (P50 = 1.1 mmHg at 20 degrees C), compared to whale and horse Mbs.
[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] 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] H-NMR study of temperature-induced structure alteration at the active site of horse h
H-NMR study of temperature-induced structure alteration at the active site of horse heart cytochrome c.
Related Articles H-NMR study of temperature-induced structure alteration at the active site of horse heart cytochrome c.
J Biochem. 1996 Jan;119(1):16-22
Authors: Yamamoto Y
The molecular structure of the active site of horse heart met-cyano cytochrome c, as a function of temperature, has been investigated using 1H-NMR. A temperature dependence study of the NMR spectra revealed that one heme methyl proton resonance exhibits anti-Curie...
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[NMR paper] Rotational resonance NMR study of the active site structure in bacteriorhodopsin: con
Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage.
Related Articles Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage.
Biochemistry. 1992 Sep 1;31(34):7931-8
Authors: Thompson LK, McDermott AE, Raap J, van der Wielen CM, Lugtenburg J, Herzfeld J, Griffin RG
Rotational resonance, a new solid-state NMR technique for determining internuclear distances, is used to measure a distance in the active site of...
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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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[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...
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[NMR paper] A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus me
A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin.
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 A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin.
Eur J Biochem. 1990 Aug 28;192(1):225-9
Authors: Yamamoto Y, Osawa A, Inoue Y, Chûjô R, Suzuki T
The ferric high-spin form of the myoglobin from the shark Galeorhinus japonicus, which...
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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...