A Putative Quantum Transition in Zinc Atoms of Flavivirus Polymerase

Abstract

Metal ions are coordinated in many proteins, and zinc ions are an obligatory attribute of several important protein families. Rna-dependent RNA polymerase (RdRp) in viruses of flavivirus genus contains two zinc atoms located in the two specific zinc binding sites. A reason which can explain a presence of zinc ions in the proteins is not as clear as for ions of another metals. A quantum transition in zinc ions is allowed and by a proposed suggestion it is utilized to arrange synchronous transformations of the coordinating proteins via a quantum entanglement. Molecular dynamics experiments which were conducted for flavivirus NS5 protein suggest that the conformation of the RdRp domain in NS5 is highly sensitive to the bond lengths between the zinc atoms and their four coordinating atoms. We hypothesize that a change of conformation is required for the functioning of the viral replicative complex and that it is the quantum transition in the zinc atoms which slightly changes the bond lengths; thus assisting the switch between the conformations. The deterministic induction of the transition in a virus replication can be explained by a quantum entanglement of the zinc atoms with some another quantum system.