draw bridge  
Science Home
  fan belt  
HOME Science Errors

ATP Theory is in Error

Biophysicists developed a theory for ATP which 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.

Biochemical energy is 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 undestood, 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.

Biochemical energy can be converted to kinetic energy, but kinetic energy can never be converted to biochemical energy, because electrons can influence the motion of nuclei, but nuclei cannot significantly influence the relative motion of electrons which orbit them. The linear motion of electrons in nonorganic systems (such as copper wires) is electrical energy, which is a totally different subject.

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.

ATP is the universal energy carrier in biology. It donates chemical energy to assist in biochemical reactions.

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.

Batteries are not a form of chemical energy; they are a form of electrical energy. Chemical energy is in bonds created by orbiting electrons. Electrical energy is in non-orbiting (linear) electrons.

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.

For example, if a nucleus needed to move ten units to affect an electron which orbits it, the electron would make thousands of orbits before the nuclei could move that much distance. So the displacement of the nucleus would be miniscule during each orbit of the electron.

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.

Since the motion of a nucleus is invisible to the electrons which orbit it, it cannot influence the energy of those electrons. If electromagnetic forces are added, they can influence electrons, but this situation applies to ionic systems and electricity, not biochemistry.

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.

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.


The process of respiration which energizes ATP consists of a series of cytochromes associated with proteins. Cytochromes are colored compounds with metals in the center. Scientists do not know the function of cytochromes.

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.

The Absurd Claims of Biophysicists

Biophysicists claim that the high energy electrons are used to create the osmotic pressure of the protons. No such mechanism exists. As protons turn proteins, ATP is said to be energized by "binding force" from the rotating proteins. This says kinetic energy is converted into chemical energy, an impossibility. It also uses as much energy as it transfers, so there can 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). It would also 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.

Therefore, according to 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.

What Really Happens

What really happens would be that an ATP molecule would be used to pump a proton into its gradient, but the proton is then used only to turn the rotating proteins. One proton would turn the proteins through numerous revolution, as very little energy would be lost in keeping the proteins rotating.

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.

The real evidence in ATP science indicates that cytochromes pick up high energy electrons and transfer lower energy electrons to the phosphate bond, while the spinning protein only moves molecules into place. To discard all that evidence and replace it with whimsical absurdity is fraud. It's not scientific error. It's too blatant of a mockery of scientific standards to be error. It's a contempt for science by power mongers who want to reduce the social standards to a level which allows them to dominate and control society.


Home Page
Science Errors
Sociology of Corruption
Home Page
Science Errors
Sociology of Corruption