Structure and Molecular Function
The flavohemoglobin protein contains two domains: an oxidoreductase FAD-binding domain, and a b-type heme-containing "globin" domain and optionally an oxidoreductase NAD-binding domain. The reductase domain supplies an electron to the heme iron to achieve a high rate of catalytic NO dioxygenation. In addition to numerous flavohemoglobins, many distantly related members of the hemoglobin superfamily including the muscle myoglobin, the non-symbiotic plant hemoglobin and symbiotic plant leghemoglobin, the neuronal neuroglobin, and the mammalian cytoplasmic cytoglobin appear to function as nitric oxide dioxygenases (NODs), although the cellular electron donor(s) for many globins have yet to be defined. Electron donors may include ascorbate, cytochrome b5 or ferredoxin reductase. The catalytic NO dioxygenation can be written in its simplest form:
- NO + O2 + e- NO3-
Catalysis is very efficient. The reported bimolecular NO dioxygenation rate constants range from 2 x 107 M−1s−1 for cytoglobin to 3 x 109 M−1s−1 for flavohemoglobin, and turnover rates range from 1 to 700 s−1. Structure, O2 binding, and reduction of globins appear optimized for a NO dioxygenase function.
Read more about this topic: Nitric Oxide Dioxygenase
Famous quotes containing the words structure and/or function:
“If rightly made, a boat would be a sort of amphibious animal, a creature of two elements, related by one half its structure to some swift and shapely fish, and by the other to some strong-winged and graceful bird.”
—Henry David Thoreau (1817–1862)
“Every boy was supposed to come into the world equipped with a father whose prime function was to be our father and show us how to be men. He can escape us, but we can never escape him. Present or absent, dead or alive, real or imagined, our father is the main man in our masculinity.”
—Frank Pittman (20th century)