2004: NO-bound myoglobin: Structural diversity and dynamics of the NO ligand
Zemojtel, T; Rini, M; Heyne, K; Dandekar, T; Nibbering, ETJ; Kozlowski, PM
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 2004, 126(7), p. 1930-1931
We used femtosecond infrared polarization spectroscopy and density functional theory in a study on the key signaling molecule nitric oxide (NO) bound to myoglobin. Our results show that after photolysis, a substantial fraction of NO recombines within the first few picoseconds. We discovered that the diatomic ligand is severely tilted in the protein and present evidence that the Fe−NO moiety can sample a wide range of off-axis tilting and bending conformations.
DOI 10.1021/ja039086x