Research Summary:

Dr. Boyers requested visit to my Laboratory at the VAMC\WLA, to see my advanced Quantum Imaging Technology allowing real time\space\color photographs documenting his data which led to his discovery of the ATP rotating molecule, and with his permission we named the discovery of our rotating energy wheels, "BOYERS WHEELS", "WHICH REVEAL THE ATP ROTATION, RELEASING 90% FREE WAVE\PARTICLE ENERGY INSIDE OF THE MITOCHONDRIA OF A CELL, ACROSS A MOLECULAR MOTHERBOARD".

Paul D. Boyer
Professor Emeritus; PhD, Biochemistry, University of Wisconsin; Postdoctoral, Stanford University; National Academy of Sciences; Rose Award of the American Society of Biochemistry and Molecular Biology; 1997 Nobel Prize in Chemistry

Research Description

Basic Features of the ATP Synthase Catalysis:

The membrane-bound ATP synthaseof animals, plants, and microorganisms is a highly conserved enzyme with unusual subunit stoichiometry and properties. In the binding change mechanism for the synthase developed by our laboratory, translocation of protons is regarded as driving conformational changes that promote release of a tightly bound ATP at one catalytic site and the tight binding of ADP and Pi at another catalytic site.

*(NOTE)* "An interesting speculation is that catalysis is accompanied by a rotational movement of catalytic subunits relative to a noncatalytic core".

Probes of Catalysis and Control:

We use a combination of chemical derivatization, nucleotide binding and other catalytic site occupancy measurements, conformational and structural probes, subunit isolation and interchange evaluations, subunit cross-linking 18O-phosphate exchange measurements, site-specific mutagenesis, and rapid mixing and rate of catalysis approaches.

*(NOTE)* "One example is the use of 2-azido ATP and ADP. These are good sub- strates that when photoactivated covalently modify nucleotide binding sites.

Another is the phosphate oxygen exchange methodology that reveals reactions occurring while substrates are still bound and whether the catalysis occurs by one of more pathways.


It might also be noted that this work was previously done by Dr. Lancelot Law Whyte and published in 1948 in his book, "The Unitary Principle in Physics and Biology", and by Dr. Leo Baranski and published in 1960 in his book, "Scientific Basis for World Civilization", the "Unitary Field Theory", and in which book Dr. Baranski gave total credit to Dr. Whyte for being the first person in the World to do a complete, definitive and valid scientific and mathematical explanation of Dr. Einstein's last great work on the Unified Field Theory", both of whom had studied with the Master, at different times and had corrected his work.

They were both trained Physicists, Mathematicians and Psychologists and even though they had both worked with Dr. Einstein, neither had met before, nor knew each other, as there was twenty-five (25) years difference in their ages. They only became friends after Dr. Baranski published his book. Subsequently, they met three times at planned five year intervals, and Dr. Baranski died under suspicious circumstances in 1971, one year before they were to meet again, Dr. Whyte would have been 82 at that time.

It is also significant that Dr. Paul Boyer started his research work on the ATP Rotating Molecule in 1960, the year that Dr. Baranski published his one and only book, and when I posed the question to Dr. Boyer in my Laboratory during his visit, did he know of Dr. Baranski or read his book, he was startled, shaken and taken aback, he spilled the coffee that he was drinking in his lap. He did not answer my question, excused himself and left my Laboratory in a hurry. To this day, he has never returned my calls nor visited my Laboratory again, and I am convinced that Dr. Boyer started his research based on the work previously done by Dr. Baranski, but to this day he has never acknowledged ever reading the book, or of knowing of Dr. Baranski's work.

Now you have the rest of the story. pb and jw

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