COVID-19:Attacks the 1-Beta Chain of Hemoglobin and Captures the Porphyrin to Inhibit Human Heme Metabolism

16 September 2021, Version 10
This content is a preprint and has not undergone peer review at the time of posting.


The novel coronavirus pneumonia is a contagious acute respiratory disease caused by the SARS-COV-2 coronavirus. The pathogenic mechanism of the novel coronavirus is unknown, which presents a significant impediment to the patient rescue. A conserved domain search strategy was utilized in this work to determine that a large number of viral proteins could bind to hemoglobin. S could bind to extracellular hemoglobin. SARS-COV-2 virus proteins interacted with porphyrins. SARS-COV-2 viruses could synthesize heme from porphobilinogen and encode all the similar enzymes required for the process. Both E and ORF3a contained heme-binding sites. ORF3a's Arg134 and E's Cys44 were the heme-iron binding sites, respectively. ORF3a also contained homologous domains to human cytochrome C reductase and bacterial EFeB protein. The molecular docking analysis revealed that ORF3a and ORF8 proteins were shown to be capable of attacking hemoglobin's 1-beta chain, whereas ORF3a was found to be effective in capturing heme for dissociation to iron and porphyrin. Deoxyhemoglobin was more susceptible to viral attack than oxidized hemoglobin. In summary, the combination of viral proteins to porphyrins and their metal compounds would improve the ability to permeate cell membranes and generate oxygen free radicals (ROS). It may be associated with viral infections and epidemic transmission. Viral proteins regulated the production and function of NO, CO and CO2 by inhibiting the activity of hemoglobin, thereby affecting immune cell function. Viral proteins' attack on hemoglobin could result in symptoms such as respiratory distress and blood clotting, damage to numerous organs and tissues, and disruption of normal human heme metabolism.


Novel Coronavirus
Respiratory distress
Cytokine Storm


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