The Reactions that Increase and Decrease Co2 Concentration During Viral Infection Like Covid-19 Virus: the Effect of Vitamin C

Abstract

It is known that some patients do not show any disease symptoms. The human body can resist all kinds of viruses. However, the immune system must be resistant to this virus. In viral infection treatment processes, developing an antiviral drug against the virus should be the second option. The first option is to support the immune system, so as to block propagation medium of virus. The main purpose of this study is to determine whether the vitamin C given to the patient is sufficient to prevent the formation of low pH environment that accelerates spread of virus. For this reason, the CO2 molecule must be easily separated from human body. Viral RNA viruses indirectly affect the carbonic anhydrase-9 enzyme, working on transmembrane, known as a pH-regulating enzyme. Interaction of vitamin C with oxidants has been shown to inhibit carbonic anhydrase-9 enzyme reactions. As a result of the interaction of vitamin C with oxidants, newly formed molecular formations affect carbonic anhydrase-9 enzyme reaction. This new molecule blocks the amino acids to which zinc, which is the coenzyme of the enzyme, binds.

Keywords

• Covid-19,Carbonic Anhydrase Enzyme,, Vitamin C

References

1. 1. Harri Hemilä, Vitamin C intake and susceptibility to pneumonia, The Pediatric Infectious Disease Journal: 1997, 16, 9, 836-837.
2. 2. Majid Rezaei Basiri, Theory about Treatments and Morbidity Prevention of Corona Virus Disease (Covid-19), Journal of Pharmacy and Pharmacology, 2020, 8, 89-90.
3. 3. Richard Z. Cheng, Can early and high intravenous dose of vitamin C prevent and treat coronavirus disease 2019 (COVID-19)?, Medicine in Drug Discovery, 2020 (in press.)
4. 4. Anitra C. Carr, a new clinical trial to test high-dose vitamin C in patients with COVID-19, Critical Care (2020) 24:133.
5. 5. Abel Ang, Juliet M. Pullar, Margaret J. Currie and Margreet C.M. Vissers, Vitamin C and immune cell function in inflammation and cancer, Biochemical Society Transactions (2018) 46 1147–1159.
6. 6. Carr, Anitra C, and Silvia Maggini, Vitamin C and Immune Function, Nutrients, 2017, 9, 11, 1211, doi:10.3390/nu9111211.
7. 7. Hrvoje Jakovac, COVID-19 and vitamin D—Is there a link and an opportunity for intervention?, Am J Physiol Endocrinol Metab 318: E589, 2020.
8. 8. Majid Teymoori‐Rad, Fazel Shokri, Vahid Salimi, Sayed Mahdi Marashi, The interplay between vitamin D and viral infections, Rev Med Virol. 2019;29: e2032.

9. 9. Alba Panarese, Endrit Shahini, Letter: Covid-19, and vitamin D, Aliment Pharmacol Ther. 2020;00: 1–3.
10. 10. Mahmoud Kandeel, Mohammed Al-Nazawi, Virtual screening and repurposing of FDA approved drugs against COVID-19 main protease, Life Sciences, 2020, 251, 117627.
11. 11. Manli Wang, Ruiyuan Cao, Leike Zhang, Xinglou Yang, Jia Liu, Mingyue Xu, Zhengli Shi, Zhihong Hu, Wu Zhong and Gengfu Xiao, Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro, Cell Research, 2020, 30, 269–271.
12. 12. Rosa SGV and Santos WC. Clinical trials on drug repositioning for COVID-19 treatment. Rev Panam Salud Publica. 2020, 44: e40.
13. 13. Roger Meli, Thomas Nauser, Petr Latal, Willem H. Koppenol, Reaction of Peroxynitrite with Carbon Dioxide: Intermediates and Determination of the Yield of CO3- and NO2, J. Biol. Inorg. Chem., 2002 7, 31-36.
14. 14. Sandra Serrano-Luginbuehl, Reinhard Kissner, and Willem Hendrik Koppenol, The Reaction of CO2 with ONOO-. One Molecule of CO2 is not Enough, Chem. Res. Toxicol. 2018, 31, 8, 721-730.
15. 15. Houwen Zhang, Giuseppe L. Squadrito, and William A. Pryor, The Mechanism of the Peroxynitrite–Carbon Dioxide Reaction Probed Using Tyrosine, Nitric Oxide: Biology and Chemistry, 1997, 1, 4, 301–307.
16. 16. William A. Pryor, Jean-Noe¨L Lemercier, Houwen Zhang, Rao M. Uppu, And Giuseppe L. Squadrito, The Catalytic Role of Carbon Dioxide in The Decomposition of Peroxynitrite, Free Radical Biology & Medicine, 1997, 23, 2, 331–338.
17. 17. Z. Pengt and Kenneth M. Men, Jr., Theoretical Investigation of the CO2 +OH-  HCO3- Reaction in the Gas and Aqueous Phases, J. Am. Chem. SOC. 1993,115, 9640-9647.
18. 18. Rossana Occhipinti, Walter F. Boron, Role of Carbonic Anhydrases and Inhibitors in Acid–Base Physiology: Insights from Mathematical Modeling, Int. J. Mol. Sci. 2019, 20, 3841; doi:10.3390/ijms20153841.
19. 19. E. Kupriyanova, N. Pronina, and D. Los, Carbonic anhydrase – a universal enzyme of the carbon-based life, Photosynthetica, 2017, 55, 3-19.
20. 20. Jean-Yves Winum, Carbonic anhydrase enzymes for regulating mast cell hematopoiesis and type-2 inflammation: a patent evaluation (WO2017/058370), Expert Opinion on Therapeutic Patents, 2018, DOI: 10.1080/13543776.2018.1501472.
21. 21. Büşra Tezcan, Nejla Mendil Erdoğan, Özcan Erdemli, Transfüzyon İkileminin Çözümü:Doku Oksijenasyonu ve Kritik Hemoglobin, Acıbadem Universitesi Sağlık Bilimleri Dergisi, 2015, 6, 1.
22. 22. Anitra Carr and Balz Frei, Does vitamin C act as a pro-oxidant under physiological conditions, The Faseb Journal, 1999, 1007-1024.
23. 23. Man Nien Schuchmann and Clemens von Sonntag, Determination of the Rate Constants of the Reactions CO2 +OH-  HCO3— and Barbituric Acid -> Barbiturate Anion + H+ Using the Pulse Radiolysis Technique, Zeitschrift für Naturforschung B, 37,9, 2014.
24. 24. Anthony J. Nappi and Emily Vass, Hydroxyl Radical Production by Ascorbate and Hydrogen Peroxide, Neurotoxicity Research, 2012, 2, 343-355.
25. 25. Frisch, M.J.; Trucks, G.W.; Schlegel, H.B.; Scuseria, G.E.; Robb, M.A.; Cheeseman, J.R.; Scalmani, G.; Barone, V.; Mennucci, B.; Petersson, G.A.; Nakatsuji, H.; Caricato, M.; Hratchian, X. Li,H.P.; Izmaylov, A.F.; Bloino, J.; Zheng, G.; Sonnenberg, J.L.; Hada, M.; Ehara, M.; Toyota, K. ; Fukuda, R. ; Hasegawa, J.; Ishida, M.; Nakajima, T.; Honda, Y.; Kitao, O.; Nakai, H.; Vreven, T.; Montgomery Jr. J.A.; Peralta, J.E.; Ogliaro, F.; Bearpark, M.; Heyd, J.J.; Brothers, E.; Kudin, K.N.; Staroverov, V.N.; Kobayashi, R.; Normand, J.; Raghavachari, K.; Rendell, A.; Burant, J.C.; Iyengar, S.S.; Tomasi, J.; Cossi, M.; Rega, N.; Millam, J.M.; Klene, M.; Knox, J.E.; Cross, J.B.; Bakken, V.; Adamo, C.; Jaramillo, J. ; Gomperts, R.; Stratmann, R.E.; Yazyev, O.; Austin, A.J.; Cammi, R.; Pomelli, C.; Ochterski, J.W.; Martin, R.L.; Morokuma, K.; Zakrzewski, V.G.; Voth, G.A.; Salvador, P.; Dannenberg, J.J.; Dapprich, S.; Daniels, A.D.; Farkas, O.; Foresman, J.B.; Ortiz, J.V.; Cioslowski, J.; Fox, D.J. Gaussian 09, Revision A.1, Gaussian Inc., Wallingford CT 2009.
26. 26. DeLano, W. L. (2002). Pymol: An open-source molecular graphics tool. CCP4 Newsletter On Protein Crystallography, 40, 82-92.