Related ArticlesNMR 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
The heme molecular structure of the met-azido form of the myoglobin from the shark Galeorhinus japonicus has been investigated by 1H NMR. A nuclear Overhauser effect (NOE) was clearly observed among the heme peripheral side-chain proton signals of this complex, which undergoes thermal spin equilibrium between high-spin (S = 5/2) and low-spin (S = 1/2) states, and the NOE connectivities provided the assignment of the resonances from the heme C13(1)H2 and C17(1)H2 protons. Chemical shift inequivalence of these proton resonances not only provided information about the orientation of these methylene protons with respect to the heme plane, but also allowed characterization of the time-dependent build-up of the NOE between them, which yields the correlation time for the internal motion of the inter-proton vector. The relatively large mobility found for the C17(1)H2 group suggests that the carboxyl oxygen of the heme C17 propionate is not anchored to the apo-protein by a salt bridge. It has been shown that the ferric high-spin form of G. japonicus Mb possesses a penta-coordinated heme [Suzuki, T. (1987) Biochim. Biophys. Acta 914, 170-176; Yamamoto, Y., Osawa, A., Inoue, Y., Chûjô, R. & Suzuki, T. (1990) Eur. J. Biochem. 192, 225-229] and that the conformation of both heme propionate groups is fixed with respect to the heme, as well as the apo-protein, by a salt bridge [Yamamoto, Y., Inoue, Y., Chûjô, R. & Suzuki, T. (1990) Eur. J. Biochem. 189, 567-573]. Therefore the weakening or interruption of the interaction between the C17 propionate and His FG3 upon the changes of the coordination and spin state of the heme iron, during azide ion binding to ferric high-spin G. japonicus Mb, is attributed to the displacement of the FG corner of the apoprotein away from the heme C17 propionate group. A similar structural alteration has been revealed by X-ray structural analyses of unliganded and liganded forms of ferrous hemoproteins [Baldwin, J. & Chothia, C. (1979) J. Mol. Biol. 129, 175-220; Phillips, S.E.V. (1980) J. Mol. Biol. 142, 531-554].
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Biochim Biophys Acta. 2011 Jul 13;
Authors: Gussoni M, Scorciapino MA, Vezzoli A, Anedda R, Greco F, Ceccarelli M, Casu M
Myoglobin (Mb), the main cytosolic oxygen storage/deliver protein, is also known to interact with different small ligands exerting other fundamental physiological roles. In...
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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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05-24-2011 12:00 PM
[NMR paper] 19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes o
19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes of nitric oxide bound to the H93G cavity mutant.
Related Articles 19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes of nitric oxide bound to the H93G cavity mutant.
Biochemistry. 2001 Jul 24;40(29):8588-96
Authors: Thomas MR, Boxer SG
Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a 5- or 6-coordinate Fe--NO heme complex. The H93G mutation replaces the proximal histidine of Mb with glycine,...
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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 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] 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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08-21-2010 11:04 PM
[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...
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(2)H NMR study of the water dynamics in hydrated myoglobin.
(2)H NMR study of the water dynamics in hydrated myoglobin.
Related Articles (2)H NMR study of the water dynamics in hydrated myoglobin.
J Phys Chem B. 2010 Aug 12;114(31):10209-16
Authors: Lusceac SA, Vogel M
We use 1D and 2D (2)H NMR to study the temperature-dependent mechanism for the rotational motion of myoglobin hydration water. The results show that isotropic and anisotropic water reorientation is observed at high and low temperatures, respectively, with a continuous crossover in the temperature range of 200-230 K. The anisotropic...