Quantum criticality in bio-processes

If one simply thinks of LENR as lowering an activation barrier in a catalytic sense, then an enzymatic approach is at least feasible. If it can work, it is very likely that selection for fitness would have come up with at least some version of it. Certainly it is not commonly considered in biology, but then again no one in conventional science has really been looking.... yet. There are hydrogenases and hydrogen metabolizing microbes. They might be the place to start looking.

"[NiFe] hydrogenases: A common active site for hydrogen metabolism
under diverse conditions"

In Biochimica et Biophysica Acta Bioenergetics Volume 1827, Issues 8–9, August–September 2013, Pages 986–1002

downloadable pdf at:
http://www.sciencedirect.com/s…cle/pii/S000527281300025X

An interesting possibility is posed by the transition metal cofactors that are often, if not universally present in hydrogenases of varying sorts. Virtually all utilize NiFe.

A common theme in evolutionary biochemistry is that many enzymes and other actively functional proteins have apparently evolved to elaborate or enhance the existing chemical activities of their transition metal active site cofactors. So turning that idea around, it may be useful to examine Nickel Iron alloys or their intermetallics for useful hydrogen chemical manipulation.

Or put more briefly, perhaps we are focused too exclusively on nickel itself.

One more comment for any who might doubt the significance of biology in the search for LENR understanding:

It may be informative to consider that nature and natural selection are surely not likely to care about theory, or to be guided by such. If there are energetic advantages to be realized, the 3 X 10e9 year timescale (or possibly more if spores have ever traveled astronomical distances) gives a lot of time for nature to have effectively conducted innumerable experiments. Under the existing paradigm it is likely that bioenergetics is thought to be explainable without any nuclear chemistry. But, that is one of the problems with scientific paradigms. Vision beyond the existing paradigm is highly obscured (paraphrasing Thomas Kuhn, of course).

The LENR community may gain considerable knowledge by attending to puzzling biocatalytic facts. As I learned once in enzymology, the "active site" presumably stabilizes one or more transition states in a reaction coordinate diagram. But then there was the idea of "channeling" which allows the subcellular machinery to directly "hand off" products of one reaction to become reactants in the next.... avoiding solution dynamics and dilution, avoiding loss of concentration (Gibbs free energy is at standard concentrations, generally never the reality).

Presumably an active enzymatic site has the "tools" of spatial configuration, charge distribution, charge mobilization and surely quantized charge exchange (via either or both electron and proton), augmented by possible changes in substrate hydration, salt concentrations and so on. Add orbital resonances and other subtle QM phenomena to those "tools" ruthlessly and/or cooperatively selected for efficacy over the gigayears.