Herein we discuss surprising similarities between the operation of micron-scale active sites in condensed matter low energy neutron reactions (LENRs) and those of biological enzyme proteins. It turns-out that radiation-free LENR electroweak nuclear catalysis and enzymatic chemical catalysis are not as distant from each other as one might naively assume.
As we have explained in our many publications, LENRs are star-like, neutron-induced nuclear transmutations that produce heavier stable elements from neutron captures on lighter ones while releasing abundant quantities of clean heat during the process.
Unlike stars, fusion, and fission reactors, LENRs do not emit any deadly MeV-energy neutron and gamma radiation. They occur in microscopic domains in laboratory devices, at very low rates in some industrial processes such as pyrolysis, as well as naturally in lightning and other places elsewhere on Earth. They are quietly happening all around us but went unrecognized by legions of scientists for over 100 years because easy-to-detect hard radiation emission signatures are absent.
Importantly, LENRs can be triggered under mild macroscopic conditions; e.g. at as little as room temperature and atmospheric pressure. This enzyme-like feat is possible with electroweak catalysis which creates ultralow-energy neutrons directly from electrons and protons (hydrogen) via many-body collective quantum effects in an electroweak reaction: e + p --> n + νe.
Fried et al.’s recent stunning experimental results (“Extreme electric fields power catalysis in the active site of ketosteroid isomerase”, Science 346 pp. 1510 - 1514, Dec. 19, 2014) revealed that a structurally and compositionally complex Carbon-based isomerase enzyme protein employs a combination of very high local electric fields and quantum entanglement of particles in active sites to achieve enormous increases in chemical reaction rates. Much simpler, abiotic LENR many-body active sites comprising Q-M entangled protons and electrons achieve even more enormous catalytic increases in rates of neutron-producing electroweak reactions using exactly the same effects. A key difference between them is field-strength: the enzyme uses electric fields averaging ~1.4 x 1010 V/m; LENRs use nonequilibrium pulses > 2.5 x 1011 V/m.
It has become apparent that deep technical knowledge about details of LENR electroweak catalysis can provide valuable insights into the operation of both enzymatic and abiotic chemical catalysis. There is an opportunity to use new types of conceptual insights to help greatly increase performance and reduce costs for a broad range of important industrial catalysts.