Abstract
This article presents the original descriptions of some recent physics mechanisms (based on the thermodynamic, kinetic, and quantum tunnel effects) providing stable 2H/1H isotope fractionation, leading to the accumulation of particular isotopic forms in intra- or intercellular space, including the molecular effects of deuterium interaction with 18O/17O/16O, 15N/14N, 13C/12C, and other stable biogenic isotopes. These effects were observed mainly at the organelle (mitochondria) and cell levels. A new hypothesis for heavy nonradioactive isotope fractionation in living systems via neutron effect realization is discussed. The comparative analysis of some experimental studies results revealed the following observation: “Isotopic shock” is highly probable and is observed mostly when chemical bonds form between atoms with a summary odd number of neutrons (i.e., bonds with a non-compensated neutron, which correspond to the following equation: Nn − Np = 2k + 1, where k ϵ Z, k is the integer, Z is the set of non-negative integers, Nn is number of neutrons, and Np is number of protons of each individual atom, or in pair of isotopes with a chemical bond). Data on the efficacy and metabolic pathways of the therapy also considered 2H-modified drinking and diet for some diseases, such as Alzheimer’s disease, Friedreich’s ataxia, mitochondrial disorders, diabetes, cerebral hypoxia, Parkinson’s disease, and brain cancer.
Highlights
It is well known that many physical and chemical processes in living systems are accompanied by isotope fractionation among the atoms of biologically significant elements, primarily H, C, O, and N [1,2]
Comparative analysis of some experimental results from different scientific groups revealed the following regularity (Table 1): “Isotopic shock” is observed mostly when the formation of chemical bonds with an odd number of neutrons is highly probable, or when the system contains a chemical element, which has one or several non-compensated neutrons. The probability of such a regularity, hereinafter referred to as the neutron Basov–Dzhimak hypothesis (BADz phenomenon), was analyzed; possible mechanisms for its implementation may be connected with the ability of a non-compensated neutron to modify nuclear spins in atoms and influence the reactivity of a chemical bond formed by isotopes containing non-compensated neutrons
In a system with three neutrons, the abovementioned effect can arise because of the incapability of neutron pairs to compensate for mass fluctuations of a non-compensated neutron in an atom; in isotopes containing at least five more neutrons than the number of protons, partial mass equilibrium can occur because of the manner of distribution of these neutrons, which can decrease the intensity of the BADz phenomenon
Summary
It is well known that many physical and chemical processes in living systems are accompanied by isotope fractionation among the atoms of biologically significant elements, primarily H, C, O, and N [1,2]. It should be noted that in living organisms, intermolecular and intramolecular kinetic isotope effects will be combined, owing to a complex organization of high-molecular compounds (proteins and nucleic acids) that have high solvation ability, and because of hydrogen isotope exchange between dissociating groups in the macromolecule and its hydration shell Such changes lead to the modification of energy interactions between enzymes and substrates (intermolecular effects) but can be accompanied by intramolecular conformational rearrangements at different rates; this occurs in “enzyme–substrate” or “enzyme–cofactor (coenzyme)” complexes, which can shorten some stages of biocatalytic transformations or accelerate the transition of the enzyme into an active form after the completion of a catalytic cycle, thereby increasing the activity of biochemical processes. H which all biochemical processes of hydrogen hydrogen and oxygen that are part of an activated enzyme–substrate complex due to fixation of complex of hydrogenand andoxygen oxygenthat thatare arepart partofofan anactivated activatedenzyme–substrate enzyme–substrate complex due due to to fixation fixation of of
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