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.
Addendum:
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.
end.......re: pb and jw
