New view on the compatibility of hemoglobin function in the erythrocytes
1
Obtetrics and Gynecology, Danylo Halytsky Lviv National Medical University, Ukraine
2
Department of Public Health, SUMY STATE UNIVERSITY, Ukraine
3
Department of Biochemistry, DANULO HALYTSKY LVIV NATIONAL MEDICAL UNIVERSITY, Ukraine
4
Department of Chemistry, Lviv Medical University, Ukraine
Submission date: 2023-07-25
Acceptance date: 2023-10-03
Publication date: 2024-02-23
Corresponding author
Tetiana Volodumurivna Fartushok
Obtetrics and Gynecology, Danylo Halytsky Lviv National Medical University, Pekarska, 79010, Lviv, Ukraine
Obtetrics and Gynecology, Danylo Halytsky Lviv National Medical University, Pekarska, 79010, Lviv, Ukraine
Wiadomości Lekarskie 2024;77(1):9-16
KEYWORDS
TOPICS
ABSTRACT
Aim:
The aim of our research is to study the process of hemoglobin oxidation and the enzymatic reactions associated with it.
Material and methods:
Heparinized human blood (15 IU/ml) was obtained from the clinical department . The concentration of oxy- and methemoglobin, auto-oxidation of hemoglobin was determined spectrophotometrically spectrophotometrically. Autooxidation of hemoglobin was recorded spectrophotometrically, and protein concentration was determined by the Lowry method. Monooxygenase activity of hemoglobin was also measured by the method described by Lowry spectrophotometrically.
Results:
The obtained experimental data allow us to propose a mechanism of "spontaneous autooxidation" of oxyhemoglobin, which can be described by the following equations: Hb2+O2 Hb3+ + O2- (1) Hb2+O2 + 2e - + 2H+ Hb3+ + H2O2 (2) Hb2+O2 + 2e - + 2H+ Hb2+ + H2O2 (3) Hb2+ + O2 Hb2+O2 (4)
Conclusions:
In addition to the main, previously known functions of hemoglobin (gas transport, peroxidase, monooxygenase), it catalyzes a two-electron oxidase reaction in which O2 is reduced to H2O2. This is confirmed by experimental data on the formation of one of the products of "spontaneous autoxidation" of oxyhemoglobin ₋ deoxyform at pH 5.6 ₋ 8.9.
The aim of our research is to study the process of hemoglobin oxidation and the enzymatic reactions associated with it.
Material and methods:
Heparinized human blood (15 IU/ml) was obtained from the clinical department . The concentration of oxy- and methemoglobin, auto-oxidation of hemoglobin was determined spectrophotometrically spectrophotometrically. Autooxidation of hemoglobin was recorded spectrophotometrically, and protein concentration was determined by the Lowry method. Monooxygenase activity of hemoglobin was also measured by the method described by Lowry spectrophotometrically.
Results:
The obtained experimental data allow us to propose a mechanism of "spontaneous autooxidation" of oxyhemoglobin, which can be described by the following equations: Hb2+O2 Hb3+ + O2- (1) Hb2+O2 + 2e - + 2H+ Hb3+ + H2O2 (2) Hb2+O2 + 2e - + 2H+ Hb2+ + H2O2 (3) Hb2+ + O2 Hb2+O2 (4)
Conclusions:
In addition to the main, previously known functions of hemoglobin (gas transport, peroxidase, monooxygenase), it catalyzes a two-electron oxidase reaction in which O2 is reduced to H2O2. This is confirmed by experimental data on the formation of one of the products of "spontaneous autoxidation" of oxyhemoglobin ₋ deoxyform at pH 5.6 ₋ 8.9.
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