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Various Science  4

 
ATP Theory is in Error

 

Over the past century, biochemists determined the complex mechanism of respiration with a high degree of refinement. Then the power mongers decided to do a relativity job on the subject and put biophysicists to work on it. They turned the whole subject into a fraudulent mess with no relationship to the biochemistry involved.

The biophysicists' theory for ATP contradicts principles of chemistry. They have kinetic energy restoring the chemical energy of ATP. A truism is that kinetic energy can never be converted to biochemical energy. Kinetic energy is in the motion of nuclei; biochemical energy is in the motion of electrons.

ATP is the universal energy carrier in biology. It assists biochemical reactions by donating chemical energy.

Since animals need a lot of energy for motion, a very efficient and high-speed mechanism evolved for generating ATP. The efficiency was created through porphyrin rings exchanging electrons; and the speed was created through rotating proteins which move reactants into place and then out of the way.

All other reactions in cells depend upon diffusion to move reactants around, which is a very slow process. But the rotating proteins are very demanding to produce and use, so only ATP synthesis uses them.

Respiration is the term for the mechanism of high-speed ATP synthesis. The sequence of reactions for respiration were determined in much detail over the past century. But a couple of decades ago, the whole process was turned into chaos through fraud.

The way respiration works is that a high energy electron is donated by an NADH molecule. That electron spins through three porphyrin rings to energize an ATP molecule for each one. The net result is three ATP molecules energized for each NADH molecule.

Electron Transport Chain

Biophysicists crossed all of that out and said the ATP is energized by rotary motion of proteins which transfers energy through "binding force." Binding force on rotating proteins would be kinetic energy, not chemical energy.

Biochemical energy is stored in covalent bonds, which means electrons orbiting the bonded nuclei. The energy is in the motion of electrons. Kinetic energy is in the motion of nuclei.

covalent bonds

The ionic bonds of inorganic chemistry are different from the covalent bonds of organic chemistry. Ionic bonds are not understood, but they are weak and do not involve electrons orbiting nuclei in a close and strict manner. They are subject to electrochemical influences which organic molecules are not.

Only the radiation of photosynthesis can increase chemical energy in biological systems. All other reactions reduce the amount of chemical energy, as heat is a byproduct of energy transfers.

That's because radiation can bump an orbiting electron on one side of its orbit, when the frequency is just right. Repeated bumps can increase the energy of orbiting electrons significantly. At the wrong frequency, both sides of an electron orbit would be bumped, which would remove the energy that was added.

The linear motion of electrons in nonorganic systems (such as copper wires) is electrical energy, which is a totally different subject.

ATP gives up its energy by splitting into ADP and inorganic phosphate (Pi). To become reenergized, another source of chemical energy is needed. During respiration, the source is hydrogen attached to NAD, which is at a higher energy state than ATP. In fact, three ATPs are usually reenergized from each NADH.

Osmotic Pressure of Protons

During respiration, hydrogen ions (protons) are pumped across a membrane into an area where they form an osmotic pressure. They then pass back through the membrane while going through a protein complex causing it to rotate. As it rotates, it picks up ADP and Pi, pulls them together and then releases reconstructed ATP.

Laws of physics say that to form the bond between ADP and Pi, an outside source of high energy electrons has to be used. But biophysicists omit any such source in their theory. They say the binding site adds the increased energy.

Supposedly, the binding site picks up kinetic energy from the rotating wheel. It then creates a force which increases the energy state of the electrons which bind ADP to Pi.

The Physics of Kinetic and Chemical Energy

The pool of protons would be used only to cause rotation of the turning wheel, not as a source of energy.

Here's the physics of the subject. An osmotic gradient is a source of kinetic energy. Kinetic energy means a mass moves. Protons are mass which move across the osmotic gradient and eventually turn the wheel.

A truism is that kinetic energy cannot be transformed into biochemical energy, because force or motion of nuclei cannot be directly converted to force or motion of electrons which orbit nuclei in the close and strict manner of covalent bonds. (Stress force is generally referred to as potential energy; but still, it can only be converted to kinetic energy, not biochemical energy.)

Biochemical energy is a relationship between an electron and the nuclei that it orbits. It always moves down hill in chemical reactions except where radiant energy is added through photosynthesis.

Differences in Velocities

There can never be exceptions to these principles, and here's why. Electrons orbit nuclei at about 108 cm/s. Their extremely low mass allows them to move at such high velocity.

By contrast, nuclei (including protons) are heavy and move at low velocity compared to electrons.

An electron does not see a nucleus which it is orbiting as being significantly moving. Nuclei are practically motionless relative to the higher velocity of electrons.

This principle applies to thermal energy as well as kinetic energy. Thermal energy is randomized motion of nuclei. kinetic energy is linearized motion of any mass. Randomized motion of nuclei would be as invisible to electrons as the linear motion of kinetic energy.

Energy out of Binding Force

The biophysicists, however, are trying to get biochemical energy out of binding force. Supposedly, kinetic energy from the turning protein wheel creates binding force which supplies energy to ATP.

The problem is that binding force is a stress force between nuclei. It cannot add energy to the electrons of biochemical systems. What would give up the energy? The stress force between nuclei would remain after the electron created the bond between ADP and Pi.

An erroneous assumption of the theorists appears to be that a stress force can act upon an electron and increase its energy level by accelerating it, which is absurd.

Acceleration of Electrons

Evidence shows that external forces (other than radiation) cannot significantly accelerate the electrons of biochemical systems. Normal chemical reactions show the principle. They exert forces on electrons causing them to change orbits to form bonds, and yet the energy level always decreases.

There is a logical explanation. Acceleration is time dependent. Electrons move at such high velocity that external forces cannot act for enough time to produce significant acceleration in one direction for an orbiting electron. Acceleration would have to occur during a fraction of an electron's orbit. During the other half of the orbit, a deceleration would occur. One half of an electron orbit is not enough for significant acceleration.

Electrical systems are different in that the electrons have linear motion rather than orbital motion. Therefore, a linear force can accelerate the electrons.

Radiation can add energy to orbiting electrons, because it can exert a force on the electron repeatedly during numerous orbits. The frequency of the radiation is critical, because it must synchronize with the electron orbit in order to repeatedly add force during the same part of the orbit.

So there are theoretical reasons why binding force cannot add energy to electrons, in addition to the fact that no significant energy can be given up to electrons by stress forces between nuclei.

The biophysicists who study ATP say there is also an electrostatic force in the osmotic gradient, as if it might mysteriously be converted into chemical energy. But a one-directional force cannot change the relationship between an electron and the nuclei that it orbits for reasons described above.

Cytochromes

The process of respiration which energizes ATP consists of a series of cytochromes associated with proteins. Cytochromes are colored compounds with porphyrin rings attached and metals in the center. Scientists haven't known the function of porphyrin rings; but I see an unmistakable function in distributing electrons in cytochromes; so an electron of just the right energy is donated to each ATP molecules. Doing that creates extremely high efficiency in energy transfers.

Porphyrin Ring

The porphyrin rings associated with cytochromes have numerous double bonds surrounding a metal atom such as iron, copper or cobalt. The circumstance indicates that the double bonds and metal atom allow electrons to move back and forth between orbital and linear motion. This creates a pool of electrons with various energy levels.

Cytochrome Electrons

A high energy electron from NADH goes into the cytochrome. An electron of just the right amount of energy comes out to energize ATP. The result is very high efficiency energy transfer which allows three ATP molecules to be energized from each NADH molecule.

Proof is in the Ratio of 3 ATPs per NADH

Proof that the proton gradient does not energize the ATP is in the fact that one NADH molecule always produces exactly three ATP molecules in usual systems. The cytochromes define that relationship. If the proton gradient were an intermediate step, the ratio between NADH and ATP would vary wildly based upon efficiencies.

Electron Transport Chain

There is no explanation in the garbage produced by biophysicists of how a single electron can energize three ATP molecules as occurs.

The Absurd Claims of Biophysicists

Biophysicists claim that the high energy electrons which originate with NADH are used to create the osmotic pressure of the protons. No such mechanism exists. The pressure gradient of protons is used to turn proteins, not energize ATP.

In the analysis of biophysicists, the chemical energy of NADH is used to created in the proton gradient. Doing that would use as much energy as it transfers, so there would be no increased energy in the resulting ATP.

ATP is commonly used to transport hydrogen ions (protons) across membranes. This is called the hydrogen ion pump. It is used to control pH inside of cells by excreting excess acid (hydrogen ions).

Generally speaking, everywhere the proton pump exists, which is almost in every membrane except most outer membranes of filamentous fungi, one ATP molecule is required to pump one proton across the membrane.

Therefore, the proton pump would be the way in which the osmotic pressure of protons is created for ATP synthesis. It means some ATP is used up creating the concentrated mass of protons called an osmotic gradient.

In the theory of biophysicists, the same amount of energy would be required to create the osmotic gradient as gained in the resulting ATP, and there would be no net gain in the process. It takes the energy equivalent of an ATP molecule to move a proton into place and the energy of the proton to synthesize an ATP molecule.

The real mechanism would only require one ATP molecule per proton which turns the protein wheel, while several ATP molecules could be moved around for each proton. But in the fake analysis of biophysicists, there must be one proton and one ATP molecule used for each ATP molecule generated, which means no energy increase.

That's because in the fake mechanism there is an unbroken chain between ATP moving protons and resulting motion energizing ATP. The direct link requires a one to one ratio for energy used and energy gained in ATP. But the real mechanism has no link between the energy of the protons spinning the protein wheel and the energy gained by ATP. The spinning wheel probably requires one proton for every ten or twenty ATP molecules which are moved into place. The probably disappears with the fake mechanism which requires a one to one ratio of ATP used and ATP energized, while nature was aligned upon more energy gained than used, which justifies the "probably."

The purpose of the rotating proteins is to move reactants into place and out of the way again. Every biochemical reaction would benefit from rotating proteins for moving reactants around. Otherwise, simple diffusion is required for moving reactants, and it would be much slower.

Using rotating proteins is way too demanding for most biochemical reactions, as there are a large number of proteins involved. But it's a mechanism worth the trouble for respiration, because the rate of respiration determines the amount of activity animals can produce and the speed that they can move. When muscles are heavily used, they switch from respiration to fermentation and produce ATP, because respiration cannot keep up. This means respiration is pushed to its limits in animal activity, and rotating proteins are needed to maximize the rate of respiration.

Relativity Fraud

 
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