Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins
The heme methyl resonances in a variety of high-spin, low-spin and spin-equilibrium forms of sperm whale metmyoglobin have been assigned by reconstituting myoglobin with selectively deuterated hemes. Two patterns for the heme methyl hyperfine shifts are observed, one characteristic of the low-spin s...
Published in: | Biochimica et Biophysica Acta (BBA) - Protein Structure |
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LSU Digital Commons
1980
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Online Access: | https://digitalcommons.lsu.edu/chemistry_pubs/2095 https://doi.org/10.1016/0005-2795(80)90032-X |
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ftlouisianastuir:oai:digitalcommons.lsu.edu:chemistry_pubs-3096 2023-06-11T04:17:07+02:00 Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins La Mar, Gerd N. Budd, David L. Smith, Kevin M. 1980-04-25T08:00:00Z https://digitalcommons.lsu.edu/chemistry_pubs/2095 https://doi.org/10.1016/0005-2795(80)90032-X unknown LSU Digital Commons https://digitalcommons.lsu.edu/chemistry_pubs/2095 doi:10.1016/0005-2795(80)90032-X Faculty Publications 1 H-NMR Heme-protein interaction Metmyoglobin text 1980 ftlouisianastuir https://doi.org/10.1016/0005-2795(80)90032-X 2023-05-28T18:15:43Z The heme methyl resonances in a variety of high-spin, low-spin and spin-equilibrium forms of sperm whale metmyoglobin have been assigned by reconstituting myoglobin with selectively deuterated hemes. Two patterns for the heme methyl hyperfine shifts are observed, one characteristic of the low-spin state and the other typical of the high-spin state. The two protein forms which can change the position of their spin equilibrium significantly with changing temperature exhibit the pattern of the dominant spin state component at any temperature. The different hyperfine shift patterns for the low-spin and high-spin states are concluded to arise not from different heme-protein contacts in the two spin states, but from characteristic differential sensitivities of the dominant spin transfer mechanisms to the same rhombic perturbation. © 1980. Text Sperm whale LSU Digital Commons (Louisiana State University) Biochimica et Biophysica Acta (BBA) - Protein Structure 622 2 210 218 |
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Open Polar |
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LSU Digital Commons (Louisiana State University) |
op_collection_id |
ftlouisianastuir |
language |
unknown |
topic |
1 H-NMR Heme-protein interaction Metmyoglobin |
spellingShingle |
1 H-NMR Heme-protein interaction Metmyoglobin La Mar, Gerd N. Budd, David L. Smith, Kevin M. Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins |
topic_facet |
1 H-NMR Heme-protein interaction Metmyoglobin |
description |
The heme methyl resonances in a variety of high-spin, low-spin and spin-equilibrium forms of sperm whale metmyoglobin have been assigned by reconstituting myoglobin with selectively deuterated hemes. Two patterns for the heme methyl hyperfine shifts are observed, one characteristic of the low-spin state and the other typical of the high-spin state. The two protein forms which can change the position of their spin equilibrium significantly with changing temperature exhibit the pattern of the dominant spin state component at any temperature. The different hyperfine shift patterns for the low-spin and high-spin states are concluded to arise not from different heme-protein contacts in the two spin states, but from characteristic differential sensitivities of the dominant spin transfer mechanisms to the same rhombic perturbation. © 1980. |
format |
Text |
author |
La Mar, Gerd N. Budd, David L. Smith, Kevin M. |
author_facet |
La Mar, Gerd N. Budd, David L. Smith, Kevin M. |
author_sort |
La Mar, Gerd N. |
title |
Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins |
title_short |
Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins |
title_full |
Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins |
title_fullStr |
Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins |
title_full_unstemmed |
Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins |
title_sort |
heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins |
publisher |
LSU Digital Commons |
publishDate |
1980 |
url |
https://digitalcommons.lsu.edu/chemistry_pubs/2095 https://doi.org/10.1016/0005-2795(80)90032-X |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Faculty Publications |
op_relation |
https://digitalcommons.lsu.edu/chemistry_pubs/2095 doi:10.1016/0005-2795(80)90032-X |
op_doi |
https://doi.org/10.1016/0005-2795(80)90032-X |
container_title |
Biochimica et Biophysica Acta (BBA) - Protein Structure |
container_volume |
622 |
container_issue |
2 |
container_start_page |
210 |
op_container_end_page |
218 |
_version_ |
1768375952453140480 |