  Thermogenesis by uncoupling protein (UCP) has traditionally been explained as
the dissipation of proton gradient across the inner mitochondrial membrane into
heat. Herein, we propose that UCPs, aided by the large pore and positively
charged amino acids of suspended loops, enable protonation and transport of
DROS. Thus, UCP facilitates DROS-reactions amongst themselves, forming water
and liberating heat around the inner mitochondrial membrane. Thereby, the
simple murburn scheme for biothermogenesis integrates structural information of
UCP with its attributed physiological function.
