Hemoglobin and cytochrome c. reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cells
Abstract Maintaining life (respiration), cell death (apoptosis), oxygen transport and immunity are main biological functions of heme containing proteins. These functions are controlled by the axial ligands and the redox status of the iron ion (oscillations between Fe2+ and Fe3+) in the heme group. T...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2023-09-01
|
| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-023-41858-z |
| _version_ | 1797559944926461952 |
|---|---|
| author | Halina Abramczyk Jakub Maciej Surmacki Monika Kopeć Karolina Jarczewska Beata Romanowska-Pietrasiak |
| author_facet | Halina Abramczyk Jakub Maciej Surmacki Monika Kopeć Karolina Jarczewska Beata Romanowska-Pietrasiak |
| author_sort | Halina Abramczyk |
| collection | DOAJ |
| description | Abstract Maintaining life (respiration), cell death (apoptosis), oxygen transport and immunity are main biological functions of heme containing proteins. These functions are controlled by the axial ligands and the redox status of the iron ion (oscillations between Fe2+ and Fe3+) in the heme group. This paper aims to evaluate the current state of knowledge on oxidation and oxygenation effects in heme proteins. We determined the redox status of the iron ion in whole blood (without and with anticoagulant), hemoglobin in erythrocytes, in isolated cytochrome c and cytochrome c in mitochondria of the human lung cancer cells using UV–VIS electronic absorption spectroscopy, Raman spectroscopy and Raman imaging. Here we discussed the mechanism responsible for the Q electronic absorption band spectral behavior, i.e., its splitting, and its change in extinction coefficient, as well as vibrational modifications upon oxygenation and oxidation. We compared the redox status of heme in hemoglobin of human erythrocytes and cytochrome c in mitochondria of human lung cancer cells. Presented results allow simultaneous identification of oxy- and deoxy-Hb, where 1547 and 1604 cm−1 vibrations correspond to deoxygenated hemoglobin, while 1585 and 1638 cm−1 correspond to oxyhemoglobin, respectively. Our results extend knowledge of oxidation and oxygenation effects in heme proteins. We demonstrated experimentally the mechanism of electronic-vibrational coupling for the Q band splitting. Presented results extend knowledge on oxidation and oxygenation effects in heme proteins and provide evidence that both processes are strongly coupled. We showed that retinoic acid affects the redox state of heme in cytochrome c in mitochondria. The change of the redox status of cytochrome c in mitochondria from the oxidized form to the reduced form has very serious consequences in dysfunction of mitochondria resulting in inhibition of respiration, apoptosis and cytokine induction. |
| first_indexed | 2024-03-10T17:53:25Z |
| format | Article |
| id | doaj.art-fe06a533ad3d4e48a8243e6ec2600537 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-03-10T17:53:25Z |
| publishDate | 2023-09-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-fe06a533ad3d4e48a8243e6ec26005372023-11-20T09:18:29ZengNature PortfolioScientific Reports2045-23222023-09-0113111510.1038/s41598-023-41858-zHemoglobin and cytochrome c. reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cellsHalina Abramczyk0Jakub Maciej Surmacki1Monika Kopeć2Karolina Jarczewska3Beata Romanowska-Pietrasiak4Faculty of Chemistry, Institute of Applied Radiation Chemistry, Laboratory of Laser Molecular Spectroscopy, Lodz University of TechnologyFaculty of Chemistry, Institute of Applied Radiation Chemistry, Laboratory of Laser Molecular Spectroscopy, Lodz University of TechnologyFaculty of Chemistry, Institute of Applied Radiation Chemistry, Laboratory of Laser Molecular Spectroscopy, Lodz University of TechnologyFaculty of Chemistry, Institute of Applied Radiation Chemistry, Laboratory of Laser Molecular Spectroscopy, Lodz University of TechnologyOncological Surgery Department, Medical Genetics Department, Copernicus Provincial Multidisciplinary Centre of Oncology and Traumatology in LodzAbstract Maintaining life (respiration), cell death (apoptosis), oxygen transport and immunity are main biological functions of heme containing proteins. These functions are controlled by the axial ligands and the redox status of the iron ion (oscillations between Fe2+ and Fe3+) in the heme group. This paper aims to evaluate the current state of knowledge on oxidation and oxygenation effects in heme proteins. We determined the redox status of the iron ion in whole blood (without and with anticoagulant), hemoglobin in erythrocytes, in isolated cytochrome c and cytochrome c in mitochondria of the human lung cancer cells using UV–VIS electronic absorption spectroscopy, Raman spectroscopy and Raman imaging. Here we discussed the mechanism responsible for the Q electronic absorption band spectral behavior, i.e., its splitting, and its change in extinction coefficient, as well as vibrational modifications upon oxygenation and oxidation. We compared the redox status of heme in hemoglobin of human erythrocytes and cytochrome c in mitochondria of human lung cancer cells. Presented results allow simultaneous identification of oxy- and deoxy-Hb, where 1547 and 1604 cm−1 vibrations correspond to deoxygenated hemoglobin, while 1585 and 1638 cm−1 correspond to oxyhemoglobin, respectively. Our results extend knowledge of oxidation and oxygenation effects in heme proteins. We demonstrated experimentally the mechanism of electronic-vibrational coupling for the Q band splitting. Presented results extend knowledge on oxidation and oxygenation effects in heme proteins and provide evidence that both processes are strongly coupled. We showed that retinoic acid affects the redox state of heme in cytochrome c in mitochondria. The change of the redox status of cytochrome c in mitochondria from the oxidized form to the reduced form has very serious consequences in dysfunction of mitochondria resulting in inhibition of respiration, apoptosis and cytokine induction.https://doi.org/10.1038/s41598-023-41858-z |
| spellingShingle | Halina Abramczyk Jakub Maciej Surmacki Monika Kopeć Karolina Jarczewska Beata Romanowska-Pietrasiak Hemoglobin and cytochrome c. reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cells Scientific Reports |
| title | Hemoglobin and cytochrome c. reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cells |
| title_full | Hemoglobin and cytochrome c. reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cells |
| title_fullStr | Hemoglobin and cytochrome c. reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cells |
| title_full_unstemmed | Hemoglobin and cytochrome c. reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cells |
| title_short | Hemoglobin and cytochrome c. reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cells |
| title_sort | hemoglobin and cytochrome c reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cells |
| url | https://doi.org/10.1038/s41598-023-41858-z |
| work_keys_str_mv | AT halinaabramczyk hemoglobinandcytochromecreinterpretingtheoriginsofoxygenationandoxidationinerythrocytesandinvivocancerlungcells AT jakubmaciejsurmacki hemoglobinandcytochromecreinterpretingtheoriginsofoxygenationandoxidationinerythrocytesandinvivocancerlungcells AT monikakopec hemoglobinandcytochromecreinterpretingtheoriginsofoxygenationandoxidationinerythrocytesandinvivocancerlungcells AT karolinajarczewska hemoglobinandcytochromecreinterpretingtheoriginsofoxygenationandoxidationinerythrocytesandinvivocancerlungcells AT beataromanowskapietrasiak hemoglobinandcytochromecreinterpretingtheoriginsofoxygenationandoxidationinerythrocytesandinvivocancerlungcells |