Triosephosphate Isomerase as a Quantum Logic Gate: Could quantum decoherence be toxic?

Abstract

This study presents the hypothesis that triosephosphate isomerase (TIM), a pivotal enzyme in glycolysis, functions as a quantum logic gate. Utilizing quantum mechanics, we model TIMs catalytic conversion of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P) as a quantum operation involving precise proton transfer. To explore the broader implications of this quantum behavior, we developed a quantum model to assess the impact of Sodium-glucose co-transporter 2 inhibitors (SGLT2i) on methylglyoxal formation, a toxic byproduct linked to advanced glycation end products (AGEs). Our model predicts that SGLT2i could reduce methylglyoxal by decreasing the likelihood of intermediate formation, providing a potential mechanism for their protective effects observed in clinical contexts, including vascular and renal protection in diabetes, nephropathy, and heart failure. By reframing TIM as a quantum logic gate, this study not only challenges traditional views of enzymatic function but also opens new avenues for quantum biology, offering profound implications for the future of metabolic disease research and drug development. Moreover considering methylglyoxal as a result of a quantum tunnel inefficiency, its possible to hypothesize a new "noxa patogena" explicating its action as quantum interference.