FAQ

Can We Change an Enzyme's Shape & Activity Remotely? Yes. By Resonance.

Enzyme resonance with external frequency is an intriguing concept that relates to the interaction between enzymes and electromagnetic fields. Enzymes are special molecules in our bodies that help speed up chemical reactions, allowing our cells to function properly.

Resonance, in this case, refers to a situation where an enzyme absorbs energy from an outside electromagnetic field that matches its natural frequency. Just like a guitar string that vibrates at a specific frequency when plucked, enzymes also have their unique vibrational frequencies based on their atomic and molecular makeup.

When an enzyme comes into contact with an external electromagnetic field that has the same frequency as its natural frequency, something interesting happens. The energy from the electromagnetic field is transferred to the enzyme, causing it to vibrate or change its shape. This change in shape can impact the enzyme's activity, influencing how efficiently it carries out its job of catalyzing chemical reactions.

Many studies have been conducted to study the potential of resonance in enzyme-substrate systems. Wang et al. [1] summarized their review estimating that remote-controlled enzyme technologies have been widely used in biomedical and other industries [2].

Among those studies, some show remarkable increase in enzymatic activity. Many techniques immobilize enzymes on nanoparticles, deactivating and deforming them when exposed to magnetic fields, increasing their activity by about 130% [3, 4, 5]. iNOS, CAT and Cyt P450 proteins were stimulated by extremely low frequency electromagnetic fields and their activities were changed significantly [6]. Another study shows that low frequency magnetic fields can induce a doubling in rate variations for Na, K-ATPase and Cyt. Oxidase [7]. All those studies, among many others, show that enzymatic rates can be remotely changed significantly through frequencies.

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  1. Wang, F., Liu, Y., Du, C. & Gao, R. Current Strategies for Real-Time Enzyme Activation. Biomolecules. 12, 599 (2022).
  2. Bashari, M., Jin, Z., Wang, J., Zhan, X, A novel technique to improve the biodegradation efficiency of dextranase enzyme using the synergistic effects of ultrasound combined with microwave shock. Food Sci Emerg Technol, 35, 125-132 (2016).
  3. Klyachko, N.L., et al. Changing the Enzyme Reaction Rate in Magnetic Nanosuspensions by a Non-Heating Magnetic Field. Chem. Int. Ed. 51, 12016-12019 (2012).
  4. Collins, C. B., Riskowski, R. A., & Ackerson, C. J. Radiofrequency remote control of thermolysin activity. Sci Rep. 11(1), 6070 (2021).
  5. Veselov, M. M., Uporov, I. V., Efremova, M. V., Le-Deygen, I. M., Prusov, A. N., et al. Modulation of α-Chymotrypsin Conjugated to Magnetic Nanoparticles by the Non-Heating Low-Frequency Magnetic Field: Molecular Dynamics, Reaction Kinetics, and Spectroscopy Analysis. ACS omega, 7(24), 20644–20655 (2022).
  6. Patruno, A. et al. Effects of extremely low frequency electromagnetic field (ELF-EMF) on catalase, cytochrome P450 and nitric oxide synthase in erythro-leukemic cells. Life Sci.121, 117–123 (2015).
  7. Blank, M., Soo, L. Optimal frequencies for magnetic acceleration of cytochrome oxidase and Na,K-ATPase reactions. Bioelectrochemistry. 53 (2), 171-174 (2001).

Is what you are doing something like homeopathy? No... and a little bit yes.

Homeopathy put frequencies/energies into pills. So do we. That is the only similarity. We put positive energies in pills, and a lot of it. In homeopathy, it is the opposite: Homeopathy uses dilutions of harmful compounds, so diluted that no molecules of the harmful compounds can be found in the pill. In homeopathy, only the energy of the harmful compound stays in the pills.

In our pills, there is only positive frequencies/energies. 

What is a Calibrated Energy Amplitude (CEA)?

It is a unit of measurement.

To put it simply, when you get 50 CEA in your pills, you get the equivalent of 50 mg of an energized thing. 

 It is widely recognized that frequency and amplitude variations are fundamental processes in biological systems. From Molecules function (e.g., enzymes-substrate-cofactor, etc.) to molecules generation (e.g., protein-mRNA interaction), to cells function (e.g., neuron firing) and organs functions (e.g., heart beating), they all vibrate at a certain Frequency and at a certain Amplitude. They all oscillate. They are called biological oscillators.

 Calibrating both frequency and amplitude of a biological oscillator prevents physiological dysfunctions or diseases [1]. To optimize the energies imbedded in the tablets, we alter the frequency and amplitude independently or simultaneously (see article below as another example). 

1 CEA = 1 Calibrated Energy Amplitude in1 mg (ml) of distilled water, for a specific frequency.

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[1] Qin, BW., Zhao, L. & Lin, W. A frequency-amplitude coordinator and its optimal energy consumption for biological oscillators. Nat Commun 12, 5894 (2021). https://doi.org/10.1038/s41467-021-26182-2

 

Is it possible to Apply Frequency and Amplitude Variations to biological systems?

It is widely recognized that frequency and amplitude variations are fundamental processes in biological systems. From Molecules function (e.g., enzymes-substrate-cofactor, etc.) to molecules generation (e.g., protein-mRNA interaction), to cells function (e.g., neuron firing), etc, they vibrate at a certain frequency and at a certain amplitude [1]. They oscillate and are called biological oscillators. 

The majority of biological processes are regulated by enzyme systems (that are biological oscillators). Precise control over specific enzymes creates the potential for controlling cellular processes remotely. It has been shown, for example, that the thermophilic enzyme thermolysin can be remotely activated in 17.76 MHz radiofrequency (RF) fields when covalently attached to 6.1 nm gold coated magnetite nanoparticles. Many other examples exist [2].

It is also recognized that (natural) compounds that apply specific frequencies and amplitudes to those oscillators prevent physiological dysfunctions or diseases (e.g., reducing inflammation) [1].

Enzymes conjugated to magnetic nanoparticles (MNPs) undergo changes in the catalytic activity of the low-frequency magnetic field. The very 3D of the enzyme has been changed. The magnetism, the low-frequency of the magnetism, in the nanoparticles that were "placed" on a specific site of the enzyme changed the 3D configuration of the enzyme and so, the activity of the enzyme has been changed as well. The speed of its working changed. In other words, applying low-frequency magnetism to a specific part of the enzyme can make it work well (fast) or not. 

Consequently, whether one uses magnetism or Radio Frequencies, one can apply specific frequencies (at a certain amplitude) to enzymatic systems and positively alter their reactions. Our tablets use the same theories: apply natural frequencies (at certain amplitudes) to biological oscillators.

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[1] Qin, BW., Zhao, L. & Lin, W. A frequency-amplitude coordinator and its optimal energy consumption for biological oscillators. Nat Commun 12, 5894 (2021). https://doi.org/10.1038/s41467-021-26182-2

[2] Collins, C. B., Riskowski, R. A., Ackerson, C.J. Radiofrequency remote control of thermolysin activity. Sci Rep 2021 Mar 16;11(1):6070. doi: 10.1038/s41598-021-85611-w.

 

Can a Resonance Form (with a Specific Energy Profile) Depict an Enzyme State?

Successive Bond shifts between reactant and product bonding patterns

The concept of enzyme resonance has often been based on the idea that specific frequencies can be influenced by external electromagnetic fields.  The "resonance theory" has evolved into the "natural resonance theory" (NRT) that has acquired a strong theoretical basis, backed by more and more applications and research: NRT uses “convexity-based algorithms”, dealing with chemical applications including resonance phenomena of organic chemistry and biochemistry [1].

Although traditional physical chemistry conceptions of reaction mechanism are formulated in terms of stationary points of an Arrhenius-style “energy profile” that differs sharply (in purpose and form) from the corresponding Robinson-style “arrow-pushing” mechanistic conceptions of organic chemistry, these diverse “mechanistic” conceptions can be reconciled in a unified computational protocol based on a NRT description of successive bond shifts between reactant and product bonding patterns [2]. Resonance weight can be calculated along tautomerization. As proton transfer begins, a resonance strengthens as the second structure contribution increases, then resonates in close proximity to the transition state. The transition state is then strongly delocalized [3]. As Tautomers are distinct chemical species that can be distinguished by their differing atomic connectivies, molecular geometries, and physicochemical and spectroscopic properties, this depiction might be useful for enzyme-substrate bonding patterns, but the unified theory between “energy profile” and “arrow-pushing” mechanistic conceptions might be more useful to research dealing with successive bond shifts between reactant and product bonding patterns, as well as enzyme-substrate bonding patterns. Thus, the resonance form with a specific energy profile can depict an enzyme state whose structure is a quantum superposition of frequencies from different resonance forms.

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  1. Glendening, E.D., Landis, C.R., Weinhold F. Resonance Theory Reboot. Am. Chem. Soc. 141(10) 4156-4166 (2019).
  2. Glendening, E.D., Burke, S.D., Moore, J.W. & Weinhold, F. Physiker versus Organiker Views of Reaction “Mechanism”: How Natural Resonance Theory Bridges the Gap.  Chem. Ed. 99 (11), 3702-3712 (2022).
  3. Glendening, E.D.; Weinhold, F. Pauling’s Conceptions of Hybridization and Resonance in Modern Quantum Chemistry. Molecules, 26, 4110 (2021).

 

How Can an External Vibration Increase the Activity of an Enzyme?

In 2020, Yann Chalopin showed that, in the active site of an enzyme, the stiffest parts of the enzyme scaffold (the part which is conserved throughout evolution), fast vibrations take place spontaneously [1]. Those vibrations are localized and are directly related to the enzyme’s biological function. Chapolin uses the term continuity/order to describe that area as it allows energy propagation, spreading and damping into the scaffold (noting that temperature is maintaining that function) [1]. He showed that the vibrations in the enzyme's active site (the localized vibrations) can be modulated by rate promoting vibrations (RPVs) to increase chemical rates [1]. In other words, an external vibration can increase the activity of an enzyme. That is what we do at BioEnergy Assist. 

 

  1. Chalopin, Y. The physical origin of rate promoting vibrations in enzymes revealed by structural rigidity. Sci Rep.10, 17465 (2020).