Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility
The dynamics of Hemoglobin I (HbI) from the clam Lucina pectinata, from wild-type sperm whale (SW) myoglobin, and from the L29F/H64Q/V68F triple mutant of SW, both unligated and bound to hydrogen sulfide (H2S), have been studied in molecular dynamics simulations. Features that account for difference...
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ftunivlaplata:oai:sedici.unlp.edu.ar:10915/83269 2023-05-15T18:26:45+02:00 Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility Fernandez-Alberti, S. Bacelo, D. E. Binning Jr., R. C. Echave, Julián Chergui, M. Lopez-Garriga, J. 2006 application/pdf 1698-1709 http://sedici.unlp.edu.ar/handle/10915/83269 en eng Biophysical Journal vol. 91, no. 5 http://sedici.unlp.edu.ar/handle/10915/83269 issn:0006-3495 http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) CC-BY-NC-SA Química Articulo 2006 ftunivlaplata 2020-04-05T00:00:59Z The dynamics of Hemoglobin I (HbI) from the clam Lucina pectinata, from wild-type sperm whale (SW) myoglobin, and from the L29F/H64Q/V68F triple mutant of SW, both unligated and bound to hydrogen sulfide (H2S), have been studied in molecular dynamics simulations. Features that account for differences in H2S affinity among the three have been examined. Our results verify the existence of an unusual heme rocking motion in unligated HbI that can promote the entrance of large ligands such as H2S. The FQF-mutant partially reproduces the amplitude and relative orientation of the motion of HbI's heme group. Therefore, besides introducing favorable electrostatic interactions with H2S, the three mutations in the distal pocket change the dynamic properties of the heme group. The active-site residues Gln-64(E7), Phe-43(CD1), and His-93(F8) are also shown to be more flexible in unligated HbI than in FQF-mutant and SW. Further contributions to H2S affinity come from differences in hydrogen bonding between the heme propionate groups and nearby amino acid residues. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas Article in Journal/Newspaper Sperm whale Universidad Nacional de La Plata (UNLP): SeDiCI (Servicio de Difusión de la Creación Intelectual) |
institution |
Open Polar |
collection |
Universidad Nacional de La Plata (UNLP): SeDiCI (Servicio de Difusión de la Creación Intelectual) |
op_collection_id |
ftunivlaplata |
language |
English |
topic |
Química |
spellingShingle |
Química Fernandez-Alberti, S. Bacelo, D. E. Binning Jr., R. C. Echave, Julián Chergui, M. Lopez-Garriga, J. Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility |
topic_facet |
Química |
description |
The dynamics of Hemoglobin I (HbI) from the clam Lucina pectinata, from wild-type sperm whale (SW) myoglobin, and from the L29F/H64Q/V68F triple mutant of SW, both unligated and bound to hydrogen sulfide (H2S), have been studied in molecular dynamics simulations. Features that account for differences in H2S affinity among the three have been examined. Our results verify the existence of an unusual heme rocking motion in unligated HbI that can promote the entrance of large ligands such as H2S. The FQF-mutant partially reproduces the amplitude and relative orientation of the motion of HbI's heme group. Therefore, besides introducing favorable electrostatic interactions with H2S, the three mutations in the distal pocket change the dynamic properties of the heme group. The active-site residues Gln-64(E7), Phe-43(CD1), and His-93(F8) are also shown to be more flexible in unligated HbI than in FQF-mutant and SW. Further contributions to H2S affinity come from differences in hydrogen bonding between the heme propionate groups and nearby amino acid residues. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas |
format |
Article in Journal/Newspaper |
author |
Fernandez-Alberti, S. Bacelo, D. E. Binning Jr., R. C. Echave, Julián Chergui, M. Lopez-Garriga, J. |
author_facet |
Fernandez-Alberti, S. Bacelo, D. E. Binning Jr., R. C. Echave, Julián Chergui, M. Lopez-Garriga, J. |
author_sort |
Fernandez-Alberti, S. |
title |
Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility |
title_short |
Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility |
title_full |
Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility |
title_fullStr |
Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility |
title_full_unstemmed |
Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility |
title_sort |
sulfide-binding hemoglobins: effects of mutations on active-site flexibility |
publishDate |
2006 |
url |
http://sedici.unlp.edu.ar/handle/10915/83269 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
Biophysical Journal vol. 91, no. 5 http://sedici.unlp.edu.ar/handle/10915/83269 issn:0006-3495 |
op_rights |
http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
op_rightsnorm |
CC-BY-NC-SA |
_version_ |
1766208725673050112 |