Title

Spin-dependent O2 binding to hemoglobin

College

College of Science

Department/Unit

Physics

Document Type

Article

Source Title

ACS Omega

Volume

3

Issue

8

First Page

9241

Last Page

9245

Publication Date

8-31-2018

Abstract

We report results of our study on the mechanism of spin-dependent O2 binding to hemoglobin, which we represent as FePIm (Fe = iron, P = porphyrin, Im = imidazole). This involves the transition between two states, viz., the oxyhemoglobin state and the deoxyhemoglobin state. The deoxyhemoglobin state pertains to FePIm and a free O2 molecule, while the oxyhemoglobin state pertains to an O2 bound to FePIm. The deoxyhemoglobin and oxyhemoglobin systems have triplet and singlet total magnetizations, respectively. We found that a spin transition from triplet to quintet to singlet mediates the O2 binding process, and this accelerates the reaction. We also found that the position of the Fe atom out of the porphyrin plane is an important indicator of O2 affinity. Copyright © 2018 American Chemical Society.

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Digitial Object Identifier (DOI)

10.1021/acsomega.8b00879

Disciplines

Physics

Keywords

Oxyhemoglobin; Hemoglobin; Oxygen in the body

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