Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study
NO binding to the T-state of human hemoglobin (HbA) induces the cleavage of the proximal His bonds to the heme iron in the α-chains, whereas it leaves the β-hemes hexacoordinated. The structure of the nitrosylated T-state of the W37Eβ mutant (W37E) shows that the Fe-His87α bond remains intact. Exact...
Guardado en:
| Publicado: |
2013
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v587_n15_p2393_Petruk http://hdl.handle.net/20.500.12110/paper_00145793_v587_n15_p2393_Petruk |
| Aporte de: |
| id |
paper:paper_00145793_v587_n15_p2393_Petruk |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_00145793_v587_n15_p2393_Petruk2025-07-30T17:20:25Z Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study Molecular dynamics Nitric oxide Nitrosylhemoglobin heme hemoglobin hemoglobin alpha chain hemoglobin beta chain nitric oxide article controlled study density functional theory hydration ligand binding molecular dynamics nitrosylation priority journal protein conformation protein tertiary structure Molecular dynamics Nitric oxide Nitrosylhemoglobin Hemoglobins Humans Molecular Dynamics Simulation Nitric Oxide Protein Structure, Quaternary NO binding to the T-state of human hemoglobin (HbA) induces the cleavage of the proximal His bonds to the heme iron in the α-chains, whereas it leaves the β-hemes hexacoordinated. The structure of the nitrosylated T-state of the W37Eβ mutant (W37E) shows that the Fe-His87α bond remains intact. Exactly how mutation affects NO binding and why tension is apparent only in HbA α-heme remains to be elucidated. By means of density functional theory electronic structure calculations and classical molecular dynamics simulations we provide an explanation for the poorly understood NO binding properties of HbA and its W37E mutant. The data suggest an interplay between electronic effects, tertiary structure and hydration site modifications in determining the tension in the NO-ligated T-state HbA α-chain. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. 2013 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v587_n15_p2393_Petruk http://hdl.handle.net/20.500.12110/paper_00145793_v587_n15_p2393_Petruk |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Molecular dynamics Nitric oxide Nitrosylhemoglobin heme hemoglobin hemoglobin alpha chain hemoglobin beta chain nitric oxide article controlled study density functional theory hydration ligand binding molecular dynamics nitrosylation priority journal protein conformation protein tertiary structure Molecular dynamics Nitric oxide Nitrosylhemoglobin Hemoglobins Humans Molecular Dynamics Simulation Nitric Oxide Protein Structure, Quaternary |
| spellingShingle |
Molecular dynamics Nitric oxide Nitrosylhemoglobin heme hemoglobin hemoglobin alpha chain hemoglobin beta chain nitric oxide article controlled study density functional theory hydration ligand binding molecular dynamics nitrosylation priority journal protein conformation protein tertiary structure Molecular dynamics Nitric oxide Nitrosylhemoglobin Hemoglobins Humans Molecular Dynamics Simulation Nitric Oxide Protein Structure, Quaternary Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study |
| topic_facet |
Molecular dynamics Nitric oxide Nitrosylhemoglobin heme hemoglobin hemoglobin alpha chain hemoglobin beta chain nitric oxide article controlled study density functional theory hydration ligand binding molecular dynamics nitrosylation priority journal protein conformation protein tertiary structure Molecular dynamics Nitric oxide Nitrosylhemoglobin Hemoglobins Humans Molecular Dynamics Simulation Nitric Oxide Protein Structure, Quaternary |
| description |
NO binding to the T-state of human hemoglobin (HbA) induces the cleavage of the proximal His bonds to the heme iron in the α-chains, whereas it leaves the β-hemes hexacoordinated. The structure of the nitrosylated T-state of the W37Eβ mutant (W37E) shows that the Fe-His87α bond remains intact. Exactly how mutation affects NO binding and why tension is apparent only in HbA α-heme remains to be elucidated. By means of density functional theory electronic structure calculations and classical molecular dynamics simulations we provide an explanation for the poorly understood NO binding properties of HbA and its W37E mutant. The data suggest an interplay between electronic effects, tertiary structure and hydration site modifications in determining the tension in the NO-ligated T-state HbA α-chain. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
| title |
Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study |
| title_short |
Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study |
| title_full |
Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study |
| title_fullStr |
Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study |
| title_full_unstemmed |
Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study |
| title_sort |
molecular basis of the no trans influence in quaternary t-state human hemoglobin: a computational study |
| publishDate |
2013 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v587_n15_p2393_Petruk http://hdl.handle.net/20.500.12110/paper_00145793_v587_n15_p2393_Petruk |
| _version_ |
1840324215025172480 |