Change search
ReferencesLink to record
Permanent link

Direct link
Influence of mutations at the proximal histidine position on the Fe-O-2 bond in hemoglobin from density functional theory
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK).
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK).
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK). Stockholm University, Science for Life Laboratory (SciLifeLab).
Number of Authors: 3
2016 (English)In: Journal of Chemical Physics, ISSN 0021-9606, E-ISSN 1089-7690, Vol. 144, no 9, 095101Article in journal (Refereed) Published
Abstract [en]

Four mutated hemoglobin (Hb) variants and wild type hemoglobin as a reference have been investigated using density functional theory methods focusing on oxygen binding. Dispersion-corrected B3LYP functional is used and found to provide reliable oxygen binding energies. It also correctly reproduces the spin distribution of both bound and free heme groups as well as provides correct geometries at their close vicinity. Mutations in hemoglobin are not only an intrigued biological problem and it is also highly important to understand their effects from a clinical point of view. This study clearly shows how even small structural differences close to the heme group can have a significant effect in reducing the oxygen binding of mutated hemoglobins and consequently affecting the health condition of the patient suffering from the mutations. All of the studied mutated Hb variants did exhibit much weaker binding of molecular oxygen compared to the wild type of hemoglobin.

Place, publisher, year, edition, pages
2016. Vol. 144, no 9, 095101
National Category
Chemical Sciences Physical Sciences
Identifiers
URN: urn:nbn:se:su:diva-129074DOI: 10.1063/1.4942614ISI: 000372022800032PubMedID: 26957180OAI: oai:DiVA.org:su-129074DiVA: diva2:919550
Available from: 2016-04-14 Created: 2016-04-14 Last updated: 2016-04-14Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Todde, GuidoHovmöller, SvenLaaksonen, Aatto
By organisation
Department of Materials and Environmental Chemistry (MMK)Science for Life Laboratory (SciLifeLab)
In the same journal
Journal of Chemical Physics
Chemical SciencesPhysical Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 11 hits
ReferencesLink to record
Permanent link

Direct link