A 1 H‐NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin
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 1 H‐NMR spectroscopy. Using the heme meso ‐proton (C5H, C10H, C15H and C20H) resonance shift as a diagnostic probe...
Published in: | European Journal of Biochemistry |
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Language: | English |
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Wiley
1990
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Online Access: | http://dx.doi.org/10.1111/j.1432-1033.1990.tb19219.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1990.tb19219.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1990.tb19219.x |
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crwiley:10.1111/j.1432-1033.1990.tb19219.x 2024-06-02T08:14:54+00:00 A 1 H‐NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin YAMAMOTO, Yasuhiko ŌSAWA, Akemi INOUE, Yoshio CHÛJÔ, Riichirô SUZUKI, Tomohiko 1990 http://dx.doi.org/10.1111/j.1432-1033.1990.tb19219.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1990.tb19219.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1990.tb19219.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 192, issue 1, page 225-229 ISSN 0014-2956 1432-1033 journal-article 1990 crwiley https://doi.org/10.1111/j.1432-1033.1990.tb19219.x 2024-05-03T11:15:42Z 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 1 H‐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 p K value and the rate for this acid‐alkaline transition in G. japonicus metMb were found to be ∼ 10 and ≪ 4 × 10 2 s −1 , respectively. Since the p K value of the acidalkaline 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 ≪ 1.5 × 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. Article in Journal/Newspaper Sperm whale Wiley Online Library Wyman ENVELOPE(158.950,158.950,-83.900,-83.900) European Journal of Biochemistry 192 1 225 229 |
institution |
Open Polar |
collection |
Wiley Online Library |
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crwiley |
language |
English |
description |
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 1 H‐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 p K value and the rate for this acid‐alkaline transition in G. japonicus metMb were found to be ∼ 10 and ≪ 4 × 10 2 s −1 , respectively. Since the p K value of the acidalkaline 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 ≪ 1.5 × 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. |
format |
Article in Journal/Newspaper |
author |
YAMAMOTO, Yasuhiko ŌSAWA, Akemi INOUE, Yoshio CHÛJÔ, Riichirô SUZUKI, Tomohiko |
spellingShingle |
YAMAMOTO, Yasuhiko ŌSAWA, Akemi INOUE, Yoshio CHÛJÔ, Riichirô SUZUKI, Tomohiko A 1 H‐NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin |
author_facet |
YAMAMOTO, Yasuhiko ŌSAWA, Akemi INOUE, Yoshio CHÛJÔ, Riichirô SUZUKI, Tomohiko |
author_sort |
YAMAMOTO, Yasuhiko |
title |
A 1 H‐NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin |
title_short |
A 1 H‐NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin |
title_full |
A 1 H‐NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin |
title_fullStr |
A 1 H‐NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin |
title_full_unstemmed |
A 1 H‐NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin |
title_sort |
1 h‐nmr study of electronic structure of the active site of galeorhinus japonicus metmyoglobin |
publisher |
Wiley |
publishDate |
1990 |
url |
http://dx.doi.org/10.1111/j.1432-1033.1990.tb19219.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1990.tb19219.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1990.tb19219.x |
long_lat |
ENVELOPE(158.950,158.950,-83.900,-83.900) |
geographic |
Wyman |
geographic_facet |
Wyman |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
European Journal of Biochemistry volume 192, issue 1, page 225-229 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1432-1033.1990.tb19219.x |
container_title |
European Journal of Biochemistry |
container_volume |
192 |
container_issue |
1 |
container_start_page |
225 |
op_container_end_page |
229 |
_version_ |
1800738906790952960 |