Enzymes
fold into three-dimensional structures to distribute amino
acid residues for catalysis, which inspired the supramolecular approach
to construct enzyme-mimicking catalysts. A key concern in the development
of supramolecular strategies is the ability to confine and orient
functional groups to form enzyme-like active sites in artificial materials.
This review introduces the design principles and construction of supramolecular
nanomaterials exhibiting catalytic functions of heme-dependent enzymes,
a large class of metalloproteins, which rely on a heme cofactor and
spatially configured residues to catalyze diverse reactions via a complex multistep mechanism. We focus on the structure–activity
relationship of the supramolecular catalysts and their applications
in materials synthesis/degradation, biosensing, and therapeutics.
The heme-free catalysts that catalyze reactions achieved by hemeproteins
are also briefly discussed. Towards the end of the review, we discuss
the outlook on the challenges related to catalyst design and future
prospective, including the development of structure-resolving techniques
and design concepts, with the aim of creating enzyme-mimicking materials
that possess catalytic power rivaling that of natural enzymes..