Related ArticlesA 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 possesses a Gln residue at the distal site instead of the usual His residue, has been studied by 1H-NMR spectroscopy. Using the heme meso-proton (C5H, C10H, C15H and C20H) resonance shift as a diagnostic probe for identifying the coordination system of the iron center in ferric high-spin form of hemoprotein, it has been shown that G. japonicus metmyoglobin (metMb) possesses the pentacoordinated active site. The pH-dependence study of NMR spectra of G. japonicus metMb revealed the appearance of the hydroxyl form of metMb at high pH, indicating that the protein undergoes the transition between the acidic and alkaline forms. The pK value and the rate for this acid-alkaline transition in G. japonicus metMb were found to be approximately 10 and much less than 4 x 10(2) s-1, respectively. Since the pK value of the acid-alkaline transition for the pentacoordinated heme in Aplysia limacina metMb is 7.8 [Giacometti, G.M., Das Ros, A., Antonini, E. & Brunori, M. (1975) Biochemistry 14, 1584-1588] and that of the hexacoordinated heme in sperm whale metMb is 9.1 [Brunori, M., Antonini, E., Fasella, P., Wyman, J. & Rossi-Fanelli, A. (1968) J. Mol. Biol. 34, 497-504], the OH- affinity of the ferric heme iron does not appear to depend on its coordination system. The acid-alkaline transition rate in A. limacina metMb was reported to be much less than 1.5 x 10(2) s-1 [Pande, U., La Mar, G.N., Lecomte, J.T.J., Ascoli, F., Brunori, M., Smith, K.M., Pandey, R.K., Parish, D.W. & Thanabal, V. (1986) Biochemistry 25, 5638-5646] and therefore a slow transition rate may be unique to the pentacoordinated active site of Mb.
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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[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] 1H-NMR comparative study of the active site in shark (Galeorhinus japonicus), horse,
1H-NMR comparative study of the active site in shark (Galeorhinus japonicus), horse, and sperm whale deoxy myoglobins.
Related Articles 1H-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...
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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...
A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus me
Linear Mode
