His ambition might be too big at this stage.

Hydride transfer within or between redox enzymes are at least partially promoted by mechanisms that "old" text book version of potential energy and transition-state theory (in enzyme kinetics) are found difficult to explain. And this is a new field in enzymology.

The observation of hydride transfer is technically challenging. X-ray crystallography is not very useful in this case (if one is lucky enough in getting good quality crystals and perfect x-ray diffraction, he could see fuesed electron desities between donnors and acceptors by time-resolved protein x-ray crystallography, but that also depends on how long the observer can pay to stay on the synchrotron line).

Within the next 20 years, EPR might become more helpful in identifying interactions between atoms in the active centres of redox proteins.

A new idea can be rapidly generated, but it takes much much longer for physical/experimental evidence to back it up.