Metalloenzymes

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Page author;
Thomas Squire

Metalloproteins are abundant in nature where it is estimated that

they are present in around half of all proteins. They are defined by
having at least one metal ion present within the protein.
Metalloenzymes form a subgroup within the metalloprotein grouping
and are defined by playing an active role in a catalytic process. Not
all metalloproteins are metalloenzymes, some metal ions present in
metalloproteins play a structural role for example, allowing the
protein to fold around the metal ion (e.g. Zn fingers).

Cartoon
representation of the Cys2His2 zinc finger
(image author; Thomas Splettstoesser)
Examples of natural metalloenzymes include hydrogenases, which
breaks down diatomic hydrogen atoms with a catalytic site
containing a single Fe ion or a combination of Fe-Fe or Fe-Ni ions.
This hydrogenation reaction is a very common transformation but
for chemical synthesise, it usually relies on precious metal Pt or Pd
catalysts.
Another example is nitrogenase a metalloenzyme which catalyses
the breakdown of the strong diatomic nitrogen triple bond to form
ammonia. The catalytic site involves a cluster of 7 Fe ions and
sulphur atoms around a central Mo ion. The equivalent industrial
process is the Haber (-Bosch) process, which is used to produce
fertiliser and is one of the highest energy consuming/CO2 producing
processes in modern industrial chemical production.

Nitrogenase active sites

Understanding how complex metalloenzymes (or specifically their

complex active sites) function to catalyse synthetically demanding
reactions such as those described above, highlights how
researchers can draw upon nature to develop next generation
catalysts.