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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Autores principales: Fernandez-Alberti, S., Bacelo, D. E., Binning Jr., R. C., Echave, Julián, Chergui, M., Lopez-Garriga, J.
Formato: Articulo
Lenguaje:Inglés
Publicado: 2006
Materias:
Química
Hemoglobin
Mutations
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/83269
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-83269
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Hemoglobin
Mutations
spellingShingle Química
Hemoglobin
Mutations
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
Hemoglobin
Mutations
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.
format Articulo
Articulo
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
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AT echavejulian sulfidebindinghemoglobinseffectsofmutationsonactivesiteflexibility
AT cherguim sulfidebindinghemoglobinseffectsofmutationsonactivesiteflexibility
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bdutipo_str Repositorios
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