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Measuring electron transport (ETp) across proteins in the solid-state offersa way to study electron transfer (ET) mechanism(s) that minimizes solvationeffects on the process. Solid state ETp is sensitive to any static(conformational) or dynamic (vibrational) changes in the protein. Ourmacroscopic measurement technique extends the use of ETp meas-urements down tolow temperatures and the concomitant lower current densities, because thelarger area still yields measurable currents. Thus, we reported previously asurprising lack of temperature-dependence for ETp via the blue copper proteinazurin (Az), from 80K till denaturation, while ETp via apo-(Cu-free) Az wasfound to be temperature de-pendent \geq 200K. H/D substitution (deuteration)can provide a potentially powerful means to unravel factors that affect the ETpmechanism at a molecular level. Therefore, we measured and report here thekinetic deuterium isotope effect (KIE) on ETp through holo-Az as a function oftemperature (30-340K). We find that deuteration has a striking effect in thatit changes ETp from temperature independent to temperature dependent above180K. This change is expressed in KIE values between 1.8 at 340K and 9.1 at\leq 180K. These values are particularly remarkable in light of the previouslyreported inverse KIE on the ET in Az in solution. The high values that weobtain for the KIE on the ETp process across the protein monolayer areconsistent with a transport mechanism that involvesthrough-(H-containing)-bonds of the {\beta}-sheet structure of Az, likely thoseof am-ide groups.

Marked changes in electron transport through the blue copper protein azurin in the solid state upon deuteration