An atomistic view on human hemoglobin carbon monoxide migration processes.

Abstract:

:A significant amount of work has been devoted to obtaining a detailed atomistic knowledge of the human hemoglobin mechanism. Despite this impressive research, to date, the ligand diffusion processes remain unclear and controversial. Using recently developed computational techniques, PELE, we are capable of addressing the ligand migration processes. First, the methodology was tested on myoglobin's CO migration, and the results were compared with the wealth of theoretical and experimental studies. Then, we explored both hemoglobin tense and relaxed states and identified the differences between the α-and β-subunits. Our results indicate that the proximal site, equivalent to the Xe1 cavity in myoglobin, is never visited. Furthermore, strategically positioned residues alter the diffusion processes within hemoglobin's subunits and suggest that multiple pathways exist, especially diversified in the α-globins. A significant dependency of the ligand dynamics on the tertiary structure is also observed.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Lucas MF,Guallar V

doi

10.1016/j.bpj.2012.01.011

subject

Has Abstract

pub_date

2012-02-22 00:00:00

pages

887-96

issue

4

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(12)00084-7

journal_volume

102

pub_type

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