Nitric oxide (NO)
is an important signaling molecule that is involved
in a wide range of physiological and pathological events in biology.
Metal coordination chemistry, especially with iron, is at the heart
of many biological transformations involving NO. A series of heme
proteins, nitric oxide synthases (NOS), soluble guanylate cyclase
(sGC), and nitrophorins, are responsible for the biosynthesis, sensing,
and transport of NO. Alternatively, NO can be generated from nitrite
by heme- and copper-containing nitrite reductases (NIRs). The NO-bearing
small molecules such as nitrosothiols and dinitrosyl iron complexes
(DNICs) can serve as an alternative vehicle for NO storage and transport.
Once NO is formed, the rich reaction chemistry of NO leads to a wide
variety of biological activities including reduction of NO by heme
or non-heme iron-containing NO reductases and protein post-translational
modifications by DNICs. Much of our understanding of the reactivity
of metal sites in biology with NO and the mechanisms of these transformations
has come from the elucidation of the geometric and electronic structures
and chemical reactivity of synthetic model systems, in synergy with
biochemical and biophysical studies on the relevant proteins themselves.
This review focuses on recent advancements from studies on proteins
and model complexes that not only have improved our understanding
of the biological roles of NO but also have provided foundations for
biomedical research and for bio-inspired catalyst design in energy
science.