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Article

Influence of mutations at the proximal histidine position on the Fe-O2 bond in hemoglobin from density functional theory.

The Journal of chemical physics - 7 Mar 2016

Todde Guido, Hovmöller Sven, Laaksonen Aatto

Abstract excerpt

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...

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PMID: 26957180
DOI: 10.1063/1.4942614

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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