ENERGISING WATER MOLECULE COMPOSITION

SRINIVASAN GOPALAKRISHNAN

Inventor of “Process for Molecular Engineering of Materials and a Synthesizer for Molecular Engineering”.

(Indian Patent No.200286,U.K.Patent No.GB 2397782,Canada Patent No.2464955,Philippines Patent no.1-2002-000238,

pending in  U.S.A, China, Japan and in other countries)

                        Hydrogen bonding of water molecules provides unique solvent with properties essential to many physical, chemical, and biological processes. Hydrogen bond, the faint force between hydrogen and the more electronegative oxygen, is known to have vibrational phases that may be excited by numerous forms of energy transfer.

                        HYDRODRIVE’S patented PROCESS FOR MOLECULAR ENGINEERING OF MATERIALS and SYNTHESIZER cum ELECTRONIC CATALYTIC CONVERTOR is one such device capable of exciting water for energy transfer apart from exciting several other liquids, petroleum fuels, molecules of solids and gases in appropriate physical states.

            The vibrational excitation of hydrogen bonds in water is at the basis of fundamental processes such as the ability of molecules to dissolve in water, the motion of protons and other charges in water, and biological processes such as protein folding, proton transfer across the surface of proteins, and the like.

                        Due to the activation and molecular engineering process, the structure and hydrogen bonding behaviors of the water changes. The “activated water” can be used in a multitude of applications such as medicine, peptide synthesis, agriculture, printing, emulsified fuels, bio-fuel synthesis, syn-gas synthesis, hydrogen production, enhancement of fuel cells performance, emulsion paints etc.

HOW WATER MOLECULE IS ENERGISED ?.

                   A system for directly activating water molecule composition to produce excited water is described below.

                        Water composition is humidified as carrier gas- as water aerosol composition, water vapor, or a combination thereof, including micron-size, nano-size water droplets suspended in the carrier gas and passed through HYDRODRIVE’S patented SYNTHESIZER cum ELECTRONIC CATALYTIC CONVERTOR doing excitation by directly irradiating the water molecule composition to provide energized water and a control system regulates the power supply for the waves and the temperature of the electromagnetic radiation and the electric field component within the wave guide of the synthesizer to irradiate the water molecule composition.

                        The energized water comprise of excited state clathrate structures.

                        The carrier gas may be air, O₂, Ar, N₂, CO, propane, butane, LPG ,natural gas or any petroleum gas, steam and the water composition can be any emulsified fuel or bio-fuel, hydrogen peroxide solution/vapour  or molecules of any materials and liquids.

HOW ENERGISED WATER MODULATE REACTIONS ?.

PROTEIN MODULATION:

                        The physiologic process of a biological subject is associated with aquaporin-mediated water transport. By delivering energized water to a region of the biological subject associated with aquaporins, the physiologic process of a biological subject can be manipulated. The activated water modify the behaviors of hydrogen bonds in biomolecules (e.g., proteins), redox-sensitive substances, bulk water, water-mediated biological processes or protein-mediated biological processes.

                        Water molecule compositions treated with electromagnetic stimulation form excited state structures (e.g., clathrate structures) at the interface of water and air. Such energized water have dynamic hydrogen bond network, which can in turn influence non-treated molecules by transferring and distributing the effects to them, resulting in a modification of the function, properties (pH value, redox potential, etc) and structure of the non-treated molecules. The effects can have therapeutic impact on biological cells. “Therapeutic” generally refers to a therapeutic process which may be used in the treatment (including the prevention, diagnosis, alleviation, or cure) of a malady, affliction, condition, disease or injury in a biological subject. The effect could be applied to exert a biological response in vitro and/or in vivo.

                        Biological cells are compartments, inside of which up to several thousand chemical reactions (e.g., metabolism) could occur in any given moment. Some of these intracellular chemical reactions include reactions involving oxygen. These redox reactions, i.e., oxidation reactions and reduction reactions, change the status of the cellular environment. Thus, the value of the redox potential is indicative of certain status of a biological environment. It is known that any intracellular redox reactions influence other substances that are potentially redox-sensitive within that environment. In other words, any change in the intracellular redox potential has an influence on redox-sensitive intracellular substances. Redox-sensitive components in biological cells include proteins and the hydrogen bond network.

                        Influences in the change of redox potential could lead to a dysfunction or improvement of a function of the exposed components. In cell biology, it is known that protein denaturation can be caused by changes of the redox potential. On the other hand, certain protein functions are favorably amplified by changes of the redox potential. The same phenomenon is known to influence the function of the hydrogen bond network and other redox-sensitive components.

                        Besides the intracellular redox reactions, factors external to the cell also affect the redox potential of a biological cell. Chemical composition, pH value, conductivity, rate of saturation as well as the hydrogen bond structure itself can be modified by external influences, such as the influences created by energized water.

                        Because the energized water can cause changes in pH values, conductivity, hydrogen bonding behavior and redox potentials in its excited state structures, it may be used to modify or modulate protein functions (e.g., signal transduction), thereby providing therapeutic treatment for cancer, immune and autoimmune deficiencies, metabolic disorders, sleep apnea, oxidative stress caused diseases, cardiovascular disorders, COPD, asthma, diabetes, macular degeneration, Alzheimer\'s disease, Parkinson\'s disease and others.

                        Individual water molecules play central structural and functional roles in proteins, such as in proton transfer reactions. A pH gradient across a membrane influences the proton transfer because of their electrostatic interactions within the protein. Membrane proteins constitute about one third of the human genome and play diverse biological roles in processes such as biological energy transduction, transport of ions and polar compounds, pH regulation, signal transduction, and vesicle fusion. Interactions such as proton binding sites in a molecule, can deviate depending on their pH-titration which can be described by the Henderson-Hasselbalch equation. Biochemical processes depend on the ability of proteins to interact with nucleic acids, lipids, polysaccharides, substrate molecules, and each other. Specific molecular recognition is a prerequisite for electron transfer between redox partners, antigen recognition by the immune system, for signal transduction in cells, for the adaptation of cells to environmental conditions, and for many other physiological reactions.

                        One example of the importance is the binding of small ligands and ions such as protons to a protein (i.e., the pH titration of a protein). Structural changes that occur upon reduction can also be triggered by changing the pH. This coupling between electron and proton transfer fundamental to bio-energetic reactions. Often the energy of an energetically favorable electron transfer reaction is used to drive an energetically unfavorable proton transfer across a membrane. This coupling between electron and proton transfer can be facilitated by electrostatic interaction. The reduction of a redox-active group causes the protonation of adjacent groups. Such a mechanism is known for many proteins and termed redox-Bohr effect.

                        Water molecules ionize endothermically due to electric field fluctuations caused by nearby dipole librations resulting from thermal effects, and favorable localized hydrogen bonding; a process that is facilitated by exciting the O—H stretch overtone vibration. As shown below:

                        2H₂O→H₃O⁺+OH⁻

Ions are separated , for example, by means of the Grotthuss mechanism but normally recombine within a few femtoseconds. These ions may create order and may form stronger hydrogen bonds with surrounding water molecules. Changes in hydrogen bonding caused by clathrate formation may encourage ionization. Given that clathrate-like structures are likely a part of the normal structure of water and that excitation of hydrogen bonds will likely lead to bonds reforming in a clathrate form, it follows that the resultant presence of ions at the surface will have an effect on the apparent local pH and electrostatic potentials. Hydronium ions, H₃O⁺ inversion may require less energy than reforming hydrogen bonds which also suggests an alternative to rotation within hydrogen bonded clusters. The presence of an H₃O⁺ ion has been measured to affect the hydrogen bonding of at least 100 surrounding water molecules. This ion is very stable in liquid water. Once correctly oriented, the potential energy barrier to proton transfer is believed to be very small. After a proton has moved along a chain of water molecules, a reorientation of the hydrogen bonding must occur if similar proton movement is to proceed.

                        Lung tissue has a high demand for water movement, and in the case of aquaporins, millions of water molecules can be in direct transit through these tissue water channels. In some cases, aquaporins can control the movement of protons through their water channels. In this case, water molecules are deliberately re-oriented to preclude sequential hydrogen bonding so prevent proton transfer by the Grotthuss mechanism. Ion selectivity of the sodium channel may be affected by the size of the ion when it is hydrated by one or more water molecules.

                        Three kinds of membrane proteins have been shown to have water channels properties including aquaporins, cotransporters, and uniports. A molecular-kinetic description can be made based on macroscopic parameters such as pore size and thermodynamics. The influence of hydrogen bonds between solute and pore, and the pH dependence of permeability demonstrate the importance of, for example, the electrostatic effect. A realistic description of water transport can be made. Water movement is related to solute permeability of cotransporters and uniports as substrate transporters.

                        The main function of the lung is to allow transfer of oxygen and carbon dioxide molecules across the alveolar-capillary membrane. In order to achieve this task most efficiently, the lung must free itself of excess liquid, proteins, and other debris. Under normal conditions, there is continuous leakage of water from the alveolar capillaries into the interstitial space, which is eventually reabsorbed and restored to the circulation.

                        Aquaporins have to be highly specific for water to prevent other solutes and ions from also crossing the membrane. In this respect, protons present a particularly difficult challenge, because the positive charge of a proton can move along a column of water by hydrogen bond exchange. Since proton fluxes across cellular membranes drive physiological processes, such as membrane fusion, vesicular transport, solute transport, and ATP synthesis, proton leakage across the membrane must be avoided.

                        Blocking proton transfer is believed to require interruption of the continuous chain of hydrogen bonds along a single file of water by hydrogen-binding sites at the pore surface. In some embodiments, the interactions of the membrane with neighboring water molecules may cause a reorientation of the water molecules. For example, the oxygen atom of the water molecule may reorient to form hydrogen bonds with amido groups. This reorients the two hydrogen atoms of the water molecule which are prevented from forming hydrogen bonds with adjacent water molecules in the single-file column. The water molecule in the pore constriction can form hydrogen bonds via oxygen but not through hydrogen atoms. Thus, water molecules can permeate the pore with a minimal energy barrier, whereas transfer of protons is blocked by hydrogen-bond isolation from bulk water.

                        A large proportion of internal surface area of the lung is lined by alveolar epithelial cells. Water permeability between the airspace and vasculature in the lungs is high and water movement across the interface of airspace and lung vasculature is required to maintain the normal state of physiological processes. Water movement also may be important in maintaining lung water homeostasis. Alveolar O₂ diffuses toward the exchange surface 1.2 times faster than CO₂ leaves the exchange surface and a high water solubility coefficient promotes diffusion. Gases must be carried away to maintain local diffusion gradients in the lung. Osmotic water permeability in type I cells is also weakly temperature dependent.

                        Between the air and the vasculature there are epithelial, interstitial, and endothelial compartments. The alveolar epithelium, which covers more than 99% of the internal surface area of the lungs is comprised of a monolayer of two morphologically distinct types of cells, type I cells and type II cells. The very thin cytoplasmic extensions of type I cells cover 95-98% of the surface area of the lung. Type II cells, which cover the remaining 2-5% of the alveolar surface, are best known for their ability to synthesize, secrete, and recycle components of pulmonary surfactant. The interstitial compartment varies considerably in thickness. At its thinnest, the alveolar epithelium is separated from capillary endothelium only by a fused membrane. Intercellular tight junctions between alveolar epithelial cells are thought to provide a tight barrier between the air and blood compartments of the lung. Based on these anatomic considerations, it is thought that alveolar epithelial type I cells might play an important role in water transport. Recent data indicate that water moves rapidly between the airspace and capillaries in response to osmotic gradients. This is facilitated by a transcellular route for water movement through molecular water channels (aquaporins). A number of aquaporins have been evaluated in lung tissue including: AQP1 in capillary endothelia and some pneumocytes; AQP4 in basolateral membranes of airway epithelium; and AQP5 in apical membranes of alveolar epithelium. But the importance of these individual aquaporins in normal lung function is not known.

                        Studies of epithelial ion and fluid transport across the distal pulmonary epithelia have provided evidence that vectorial ion transport across the alveolar and distal airway epithelia is a primary determinant of alveolar fluid clearance (AFC). Reduced levels of surfactant protein have also been related to patient outcomes with lung disorders. Active Na⁺ and Cl⁻ transport drives are also critical to net alveolar fluid clearance, as demonstrated in several different species, including the human lung.

                        In the lung, as in other epithelia, ion transporters and other membrane proteins are asymmetrically distributed on opposing cell surfaces, conferring vectorial transport properties to the polarized epithelial cells. Tight junctions populate these epithelial cells near their apical surfaces, thereby sustaining apical and basolateral cell polarity. The permeability of tight junctions is dynamic and regulated, in part, by cytoskeletal proteins and intracellular Ca concentrations and by ion channels.

                        Stress on the lung processes may be caused by issues of protein hydration, boundary layer surfactants, aquaporin water transfer, fluid build up, and vapor/water surface tension boundaries. It is known that water vapor and small clusters act in different ways on lung tissue due to their surface tension. The vibrational dynamics of water interfaces and interfacial bonded OH stretch modes can demonstrate various behaviors. The variations in clathedic alignment can change the positions of free ions such that surface tension, surface pH, and electrostatic potentials will vary. Excitation of water is one source of such activity and its resultant vibrational lifetime will vary depending on the source of excitation and the phase state of the water. Vibrational excitation is followed by spectral diffusion, vibrational relaxation, bond realignments, electrostatic changes, polarization, clathrate alignment, and thermalization in the hydrogen-bonding network, all which have different time domains dependent upon the ambient conditions such as temperature, electric fields, humidity, pressure, and proximity to other large droplets or bulk water. One peculiarity of the liquid state of water is the nonequivalence of O—H groups of water molecules in hydrogen bonding. The structure of liquid water and the mechanism of its molecular mobility must be considered in this context.

                        The organization of lipid and other insoluble surfactant monolayers at the air-water interface under equilibrium conditions is well known, as the subject has been of great interest in biology, chemistry, and physics for nearly a century. Less is known about the dynamic and stressed aspects of monolayer structure and functions, especially monolayer failure, which ultimately limits the surface tension reduction possible by a given monolayer.

                        Native lung surfactant extracts adsorb to air/water interfaces rapidly to form monolayers. The lung surfactant monolayer is initially fluid-like at large areas per molecule. On compression, lung surfactant monolayers achieve near-zero surface tension. At low-ionic strength, these aggregates apparently diffuse away from the monolayer and remain in the subphase. At high-ionic strength, the alveolar structures (vesicles) remain attached to the monolayer (or at least in the immediate vicinity of the monolayer) and rapidly reincorporate into the monolayer on expansion of the film.

                        The charged domains of the multicomponent lung surfactants have a large Debye length or low subphase ionic strength and there is an electrostatic energy barrier to readsorption of the charged vesicles to the charged interface. In opposition to this electrostatic repulsion are a complicated set of hydrophobic, Van der Waals, and other attractive interactions that promote readsorption of the bilayer aggregates to the interface.

                        Surface pressure and phase behavior are related to the strength of these attractive interactions. Interactions with the monolayer depend on the magnitude of the electrostatic repulsion, which scales with the Debye length, or the distance relative to charge separation. At low salt concentrations, the Debye length is large, and vesicles diffuse away from the monolayer. At higher salt concentrations, the Debye length is small, and the interaction can even become attractive.

                        The interaction depends on the strength of the electrostatic interactions, as the attractive interactions between bilayers are much less dependent on ionic strength. Ionic strength, pH, and electrostatic interaction will have an effect on the health and optimal function of the alveolar gas/liquid interface. If the electrostatic barrier is such that the attractive interactions dominate, the rate or readsorption is enhanced, and more vesicles readsorb before they diffuse away into the subphase. The multicomponent lipid and protein lung surfactant monolayers may be enhanced or inhibited in relation to adsorption and respreading. A broad range of hydrophilic, nonionic polymers, including polyethylene glycols, dextrans, of widely varying molecular weights enable surfactants to work optimally.

                        Such polymers are known to dehydrate multilamellar lamellar phases, or induce a depletion attraction between aggregates and a surface, thereby making bilayer aggregates less stable and/or changing the height of the energy barrier. Some cationic surfactant specific proteins might provide ways around the energy barrier as they form multilayer patches that may provide locally, net positive charged docking sites for anionic surfactant adsorption. Specific proteins locate preferentially in anionic and/or fluid bilayers as well. These docking sites for readsorption suggest that it is the multiple cationic residues of these proteins that assist with stressed function.

                        Stress on the lung processes may be caused by issues of protein hydration, boundary layer surfactants, aquaporin water transfer, fluid build up, and vapor/water surface tension boundaries.

                        The flux of respiratory gases across the tissue barriers occurs entirely by passive diffusion along established partial pressure differences. In conformity with the physics of a passive process, the structural properties of the barrier influence the rate and efficiency of gas transfer. The diffusing capacity, or the conductance of the tissue barrier for oxygen for instance, correlates directly with the surface area and inversely with the thickness of the partition. The lung works to maintain a persistent balance between the forces that move water into the extravascular spaces and the biologic devices for its removal, to exchange gases and to remove proteins, contaminants, and pathogens from its surface.

                        The tissue interface is essentially comprised of a thin epithelial cell that faces water/air, an extracellular matrix/interstitial space, and an endothelial cell that fronts the blood capillary, whereby the design of the water-blood-gas barrier is highly conserved.

                        States and factors such as the degree of inflation, perfusion pressure, surface tension, and hydrostatic pressure determine the structure and organization of the connective tissue scaffold of the lung parenchyma. The relationship between epithelial fluid transport, standing osmotic gradients, and standing hydrostatic pressure gradients assumes that the volume of lateral intercellular space per unit volume of epithelium is small and the membrane osmotic permeability is greater than the solute permeability.

                        The rate of fluid reabsorption is set by the rate of active solute transport across lateral membranes. The fluid that crosses the lateral membranes and enters the intercellular cleft is driven longitudinally by small gradients in hydrostatic pressure and molecular kinetics. The small hydrostatic pressure in the intercellular space is capable of causing significant transmembrane fluid movement; however, the transmembrane effect is countered by the presence of a small standing osmotic gradient.

                        Longitudinal hydrostatic and osmotic gradients balance such that their combined effect on transmembrane fluid flow is zero, whereas longitudinal flow is driven by the hydrostatic gradient. Because of this balance, standing gradients within intercellular clefts are effectively uncoupled from the rate of fluid reabsorption, which is driven by small, localized osmotic gradients within the cells. Water enters the cells across apical membranes and leaves across the lateral intercellular membranes. Fluid that enters the intercellular clefts can, in principle, exit either the basal end or be secreted from the apical end through tight junctions. Fluid flow through tight junctions is shown to depend on a dimensionless parameter, which scales the resistance to solute flow of the entire cleft relative to that of the junction. Estimates of the value of this parameter suggest that an electrically leaky epithelium may be effectively a tight epithelium in regard to fluid flow.

                        In the normal lung, intricate anatomic arrangements coupled with elaborate physiologic mechanisms maintain the gas-exchanging surfaces moist and free of excess protein. A transient excess of water in the interstitial space is associated with an increase in lymphatic flow. Should the excess rate of formation persist or increase, the homeostasis will be out of balance. The distribution of unbalance within the lung may also be nonuniform, often favoring the central portions early in its genesis but later redistributing under the influence of gravity. A critical limitation in anatomic design is imposed by the narrow channels through which lymph passes out of the thorax into systemic veins. Accordingly, the pulmonary lymphatic system, which seems better suited to return proteins than water to the systemic circulation, may become a limiting factor in relieving stressed states of unremitting water movement into the extravascular spaces.

                        Recent data indicates that water moves rapidly between the airspace and vasculature in response to osmotic gradients. A major function of type I cells may be the maintenance of a water permselective physical barrier. The high water permeability between the airspace and vascular compartments in the lung suggests the involvement of molecular water channels (aquaporins) in water transport. The type I cells may play an important role in the high water permeability between the airspace and vasculature of the lung. The high water permeability of type I cells, and water channel functional requirements in the lung, demonstrate the important role for aquaporin-type water channels in lung physiology.

                        Water channels are expressed strongly in airway and alveolar epithelial and endothelial plasma membranes, water permeability is high across alveolar and airway epithelia, and lung water channel expression and function are developmentally regulated.

                        Thus, use of energized water and delivering the energized water to a region of the biological subject associated with aquaporins is a method of affecting a physiologic process of a biological subject.

OXIDATIVE STRESS REDUCTION:

                        Living cells (e.g., mammalian cells, animal cells, plant cells, and insect cells, as well as various species of bacteria, algae, plankton, and protozoa, and the like) are continuously exposed to reactive oxygen species (ROS) such as, for example, lipid peroxyl, superoxide, hydrogen peroxide hydroxyl radicals, and singlet oxygen. In vivo, these reactive oxygen intermediates are often generated by cells in response to, for example, aerobic metabolism, catabolism of drugs and other xenobiotics, ultraviolet and x-ray radiation, and the respiratory burst of phagocytic cells (e.g., white blood cells) when killing invading bacteria such as those introduced through wounds or as found near the alveolus of the lung tissue. Hydrogen peroxide (H₂O₂), for example, is produced during respiration of most living organisms especially by stressed and injured cells.

                        Excess reactive oxygen species such as, for example, hydrogen peroxide can react with DNA to cause backbone breakage, produce mutations, and alter and liberate bases. Another example of the ability of reactive oxygen species to injure cells is lipid peroxidation, which involves the oxidative degradation of unsaturated lipids. Lipid peroxidation is highly injurious to membrane structure and function and can cause numerous cytopathological effects.

                        Oxidative stress results in part from an imbalance between the production of the reactive oxygen species and a biological subject\'s ability to detoxify the reactive intermediates or repair the resulting damage. Oxidative stress may cause cellular damage, resulting in alteration of the redox state (e.g., depletion of nucleotide coenzymes and disturbance of sulfhydryl-containing enzymes), and saturation and destruction of the antioxidant defense and DNA repair system. For example, changes to the normal redox state can in some instances cause toxic effects through the production of peroxides and free radicals that damage cell components including proteins, lipids, and DNA. Such oxidative biochemical injury can result in the loss of cellular membrane integrity, reduced enzyme activity, changes in transport kinetics, changes in membrane lipid content, and leakage of potassium ions, amino acids, and other cellular material. Failure to restore the cellular balance of the level of oxidizing species (e.g., reactive oxygen species and reactive nitrogen species) can result in DNA damage, lipid peroxidation, loss of intracellular calcium homeostasis, and alterations in signal transduction (e.g., cellular signaling) and metabolic pathways.

                        Oxidative stress has been associated with a variety of diseases and disorders, including aging and neuronal cell death. For example, oxidative stress is associated with the pathology of numerous neurodegenerative diseases and conditions including, but not limited to, Alzheimer\'s disease, diabetic peripheral neuropathy, multiple sclerosis, amyotrophic lateral sclerosis, Huntington\'s disease, and Parkinson\'s disease. Accordingly, there exists a need to improved cellular protection and repair processes in aerobic organisms.

                        Energized clathrate structures of water that contain partial charges or hydronium ions (H₃O⁺) are likely to form bonds with hydroxyl radicals and even weaken other hydrogen bonds in their spatial influence. These properties of the hydrogen bonded environment will be particularly evident at the surface of liquid water where charges will reside and more reactive “dangling” O—H groups will be directed away from the surface. Some hydronium ions (H₃O⁺) also point away from the surface as they only poorly accept hydrogen bonds (but strongly donate three), with their oxygen atom pointing at the surface.

This would encourage these ions to sit in the surface layer, so as to combine with ROS (e.g., hydrogen peroxide).

H₂O₂+2H₃O⁺→4H₂

Thus Oxidative stress can be reduced by providing energized water; and delivering the energized water to a biological subject, whereby the hydronium ions at the excited states of the water are combined with reactive oxygen species to render the reactive oxygen species less reactive or inactive.

IN ACCELERATING CHEMICAL REACTIONS:

                        Activated water affects HYDROGEN BONDING,

                        “Hydrogen bond” refers to a non-covalent attractive force between a hydrogen attached to an electronegative atom of one molecule and an electronegative atom of a different molecule. When hydrogen bonding occurs between two molecules, it is also referred to as “intermolecular hydrogen bonding.” Typically, the hydrogen has a partial positive charge due to the electronegative atom it is attached to (e.g., oxygen in a water molecule). The positively charged hydrogen is thus attracted to an electronegative atom (e.g., oxygen, nitrogen, or fluorine) of another molecule (e.g., oxygen in another water molecule). Intramolecular hydrogen bonding occurs within a single molecule, in which a partially positively charged hydrogen atom attached to an electronegative atom in one portion of the single molecule can be attracted to another electronegative atom of another portion of the same molecule.

                        An important feature of the hydrogen bond is that it is directional, the direction being that of the shorter O—H covalent bond for water molecules (the hydrogen atom of the O—H bond is being donated to the oxygen atom of another water molecule). As a result, a given molecule is restricted in the number of hydrogen bonds it can form with neighboring molecules. For water molecules, the number is typically four. Formation of multiple hydrogen bonds between water molecules gives rise to a hydrogen bond network.

                        The hydrogen bond network is typically dynamic and the behavior and energy fluctuations therein are impacted by factors such as orientation and vibrational frequencies of the water molecules. By changing its orientation with respect to its surroundings, a water molecule may stretch or break one or more hydrogen bonds. Additionally, the O—H stretch vibrational frequencies of the water molecules strongly correlate with the strength of the hydrogen bonds.

                        Certain energy transfer to water molecules can excite or energize the O—H stretch vibrational modes of the hydrogen bonds. There exists various excited states of H₂O and the diffusion, relaxation and reorientation from the excited (or energized) states of the O—H stretch vibration will lead to a change of the hydrogen bond dynamics of liquid water.

                        The terms “excite”, “activate”, “energize”, “irradiate” or “stimulate” interchangeably refer to a process that adds a discrete amount of energy (“excitation energy”) to a system such as atom(s) and molecule(s), which results in a transition of the system from a baseline energy state (“ground state”) to one of higher energy state (“excited state”). For example, excited electronic or vibrational states usually occur following the absorption of radiation of certain frequency (e.g., that corresponds to the energy differentials between the ground state and the excited state). The excited state is typically short-lived and can return to the ground state through processes such as radiative emission (fluorescence), thermal emission (heat) and by reaction.

                        The vibrational dynamics of water in the proximity of a surface (i.e., interfacial water) demonstrate different behaviors depending on the phase/states of the water, i.e., whether the water is in liquid or gaseous phases. For liquid water, the vibrational dynamic also differs depending on whether the liquid water is bulk or confined.

                        In BULK LIQUID WATER, there exists a high concentration of near resonant O—H oscillators. As a result, these oscillators show a dipolar (Forster) energy-transfer process that is completely independent of the structural (hydrogen bond) dynamics of the liquid.           

                        LIQUID WATER IN A CONFINED GEOMETRY, on the other hand, shows significant difference in its structural characteristics from water in the bulk phase. For example, energy transfer of confined water involves a mechanism that is essentially different from the mechanism of resonant energy transfer in bulk liquid water. For confined water molecules, energy transfer occurs only after the two O—H oscillators are shifted into resonance. Thus, the energy flow within the molecule is governed completely by the rate at which hydrogen bonds are being broken and reformed, which slows down the energy transfer by a factor of about 20 in comparison with bulk water.

                        CONFINED WATER refers to liquid water confined to a particular environment, such as hydrophilic and hydrophobic surfaces, surfaces of biomolecules, porous media, air, etc. In certain applications, confined water is spherically confined due to surface tension at the water-air interface. An example of spherically confined water is water aerosol, which refers to fine droplets of water suspended in gas (e.g., air). In various applications, the droplets are micron-size (no more than in 1 cm in diameters), nano-sized (no more than 1 μm in diameters), or a combination thereof. In other applications, confined water includes water molecules surrounding biomolecules. These water molecules are typically involved in reactions and hydration of biomolecules and are located in highly confined geometries.

                        At excited states, confined water will form hydrogen bond clusters which will retain the molecular energy in the vibrational state of the bonds. Clathrate structures, in which small nonpolar molecules (typically gases) are trapped inside “cages” or “clusters” of hydrogen bond network of the water molecules, are largest and strongest at the point of their creation, and will continue to collapse to a ‘ground state’ as they interact with their environment. It is believed that confined water (such as a water aerosol) at excited states can adopt clathrate structures. Such structure is also referred to as “clustered structure” or “water clusters”.

                        Gaseous water, i.e., water vapor, is also characterized with dynamic and energized hydrogen bond network at the excited state.

                        Water molecule composition can be generated by including salts, minerals, vitamins, or one or more active agents selected from the group consisting of a pharmaceutical agent, a neutraceutical, an antioxidants, a phytochemical, and a homeopathic agent.

                        The molecules that participate in hydrogen bonding include biomolecules such as proteins and peptides or an aerobic organism associated with signal transduction. “Signal Transduction” refers to changes in biological functions as a result of energy transduction or the exposure to excited state water molecules (e.g., in clathrate structures). For instance, cellular activity is regulated by a complex network of intracellular and extracellular transduction pathways. Energy transfer at the cellular level can refer to the movement of signals from outside the cell to inside or from inside to outside. Energy transduction or signal transduction could mean any change in biophysical properties. For instance, in their normal biological function, proteins may fold into one or more specific spatial conformations, driven by interactions such as hydrogen bonding, ionic interactions, Van der Waals\' forces, and hydrophobic packing.

BULK WATER MODIFICATION :

                        The energized water can be delivered to bulk water to modify the properties . More specifically, when energized water contacts untreated (not energized) bulk water, energy transfer occurs, which may alter properties such as the pH, conductivity, redox potential of the bulk water. The modified bulk water is suitable for drinking, food industry, medicine, peptide synthesis, agriculture, printing, emulsified fuels, bio-fuel synthesis, syn-gas synthesis, hydrogen production, enhancement of fuel cells performance, emulsion paints etc where untreated bulk water is typically used.

The various phenomenon described are due to confirmations from:

1.Changes in pH of Energized Water

2.Ultra-sensitive fluorescence tests that detect changes in the pH values in energized water droplets as

   compared to untreated water droplets.

3 Enzymatic Test

    In a DNA cleavage test carried out and special observations made with a microscope for 30 minutes after the

    DNA  probe was exposed to the energized air stream, significant increase in  the enzymatic activity (DNA

    cleavage) was noticed...

4 Energy Transfer

    Energy transfer was confirmed by detecting the changes of dielectric potentials of energized air stream as

    compared to untreated air stream of water droplets.

    Untreated and energized air streams were connected to a resistive surface in a dielectric cell.

    Within the dielectric cell, a significant change in energy transfer was observed in the energized air stream as

     compared to the untreated air stream

5 Conductivity Test

    Untreated and energized air streams were connected to each of two different test cells. The test cell included

    two electrodes, semi conductive gel and a 200V pulse was transmitted over the gel.

    Voltage difference in the conductivity of the 200 volt pulse can be see at between the optically excited states

    and unexcited states with high ion saturation.

WILL ENERGISED WATER HELP TO REDUCE GLOBAL WARMING ?.

                   Energised water after deprotonation is OH rich and is an excellent oxidation source for the carbon monoxide and many reactive organic gases in the atmosphere for reducing the pollutants. Instead of depending upon the photolysis of ozone by solar radiation and reaction of  oxygen with water to form the OH radicals, we can spray deprotonated water rich with OH  which is not light/night dependent for it’s production. The following will highlight the ROLE OF OH IN ATMOSPHERE for CLEAN ENVIRONMENT.

                Oxidation in the Atmosphere is an important factor for global warming control. Many chemical compounds are emitted into the atmosphere but removal processes prevent them accumulating in the air.  Species are removed by dry deposition of gases or particles or can be incorporated into rain and removed by wet deposition.  For gas phase organic chemicals, removal is easiest if they are first oxidised to a less volatile, water soluble form.

                        Oxidation in a chemical sense does not necessarily mean a reaction with oxygen containing compounds, it is rather the loss of electrons.  However, in the air, oxidation does generally involve the reaction of a chemical species with an oxygen  containing compound. 

The three most important oxidising species in the air are:

the hydroxyl radical OH
the nitrate radical NO₃
the ozone molecule O₃

Hydroperoxy radicals (HO₂) are also important and the sum of HO₂ and OH is sometimes referred to as HO_x.