Myoglobin strikes back.
Over the last half century, myoglobin (Mb) has been an excellent model system to test a number of concepts, theories, and new experimental methods that proved valuable to investigate protein structure, function, evolution, and dynamics. Mb's function, most often considered just an oxygen repository, has considerably diversified over the last 15 years, especially because it was shown to have a role in the biochemistry of quenching and synthesizing nitric oxide in the red muscle, thereby protecting the cell. To tackle protein's structural dynamics by innovative biophysical methods, Mb has been the best prototype; laser flash technology made it possible to obtain molecular movies by time-resolved Laue crystallography (with ps resolution). This approach unveiled the complexity of the energy landscape and the structural basis of the stretched interconversion between conformational substates of a protein.
Brunori
Maurizio
M
Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Sapienza Università di Roma, Piazzale A. Moro 5, 00185 Roma, Italy. maurizio.brunori@uniroma1.it
D000818:Animals; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism; D011487:Protein Conformation; D013379:Substrate Specificity
D009211:Myoglobin; D006418:Heme; D010100:Oxygen