Electron Flow through Metalloproteins

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Abstract

Electron flow through proteins and protein assemblies in the
\nphotosynthetic and respiratory machinery commonly occurs
\nbetween metal centers or other redox cofactors that are
\nseparated by relatively large molecular distances, often in the
\n10−20 Å range. To inorganic chemists, such long-distance
\nelectron transfer was a mystery for many years, as we were
\naccustomed to close-contact models for the transition states of
\nsimple self-exchange reactions between metal ions in aqueous
\nsolution. One of our favorite reactions was the ferrous/ferric
\nself-exchange, which had been investigated thoroughly by
\nRichard (Dick) Dodson at the Brookhaven National Laboratory
\nin the 1940s (and published in Journal of the American Chemical
\nSociety in 1950). Dodson showed that the half-time for this
\nreaction was on the order of seconds, which he noted was “fast”
\nbut in today’s femtosecond world is very “slow”. Indeed, this
\nvery simple electron transfer, where no bonds are formed or
\nbroken, was found to be orders of magnitude slower than long-distance electron flow through metalloprotein molecules. How could this be?

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