Next Article in Journal
Lignin and Lignin-Derived Compounds for Wood Applications—A Review
Previous Article in Journal
Optimization of β-1,4-Endoxylanase Production by an Aspergillus niger Strain Growing on Wheat Straw and Application in Xylooligosaccharides Production
Article

The Redox Potential of the β-93-Cysteine Thiol Group in Human Hemoglobin Estimated from In Vitro Oxidant Challenge Experiments

LaTMA Laboratory for Analytical Toxicology and Metabonomics, Department of Health Sciences, Università degli Studi di Milano at “Ospedale San Paolo” v. A. di Rudinì 8, I-20142 Milano, Italy
Academic Editor: Hyun-Ock Pae
Molecules 2021, 26(9), 2528; https://doi.org/10.3390/molecules26092528
Received: 26 March 2021 / Revised: 22 April 2021 / Accepted: 23 April 2021 / Published: 26 April 2021
(This article belongs to the Section Bioorganic Chemistry)
Glutathionyl hemoglobin is a minor form of hemoglobin with intriguing properties. The measurement of the redox potential of its reactive β-93-Cysteine is useful to improve understanding of the response of erythrocytes to transient and chronic conditions of oxidative stress, where the level of glutathionyl hemoglobin is increased. An independent literature experiment describes the recovery of human erythrocytes exposed to an oxidant burst by measuring glutathione, glutathione disulfide and glutathionyl hemoglobin in a two-hour period. This article calculates a value for the redox potential E0 of the β-93-Cysteine, considering the erythrocyte as a closed system at equilibrium described by the Nernst equation and using the measurements of the literature experiment. The obtained value of E0 of −121 mV at pH 7.4 places hemoglobin as the most oxidizing thiol of the erythrocyte. By using as synthetic indicators of the concentrations the electrochemical potentials of the two main redox pairs in the erythrocytes, those of glutathione–glutathione disulfide and of glutathionyl–hemoglobin, the mechanism of the recovery phase can be hypothesized. Hemoglobin acts as the redox buffer that scavenges oxidized glutathione in the oxidative phase and releases it in the recovery phase, by acting as the substrate of the NAD(P)H-cofactored enzymes. View Full-Text
Keywords: glutathione; glutathione disulfide; glutathionyl-hemoglobin; hemoglobin; hydroperoxide; oxidative stress; red blood cell glutathione; glutathione disulfide; glutathionyl-hemoglobin; hemoglobin; hydroperoxide; oxidative stress; red blood cell
Show Figures

Figure 1

MDPI and ACS Style

Rubino, F.M. The Redox Potential of the β-93-Cysteine Thiol Group in Human Hemoglobin Estimated from In Vitro Oxidant Challenge Experiments. Molecules 2021, 26, 2528. https://doi.org/10.3390/molecules26092528

AMA Style

Rubino FM. The Redox Potential of the β-93-Cysteine Thiol Group in Human Hemoglobin Estimated from In Vitro Oxidant Challenge Experiments. Molecules. 2021; 26(9):2528. https://doi.org/10.3390/molecules26092528

Chicago/Turabian Style

Rubino, Federico M. 2021. "The Redox Potential of the β-93-Cysteine Thiol Group in Human Hemoglobin Estimated from In Vitro Oxidant Challenge Experiments" Molecules 26, no. 9: 2528. https://doi.org/10.3390/molecules26092528

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop