New functionalization of myoglobin by chemical modification of heme-propionates.
The reconstitution of myoglobin with an artificially created prosthetic group is a unique method for introducing a new chemical function into the protein. Particularly, the modification of two heme-propionates gives us an effective binding domain or binding site on the protein surface. This Account traces the design and construction of the highly ordered binding domain around the entrance of the heme pocket. The discussion includes the protein-small molecule or protein-protein recognition, electron transfer reaction within the complex, and enhancement of the chemical reactivity of the myoglobin with a substrate binding site. The synthetic approach to modifying a protein will be a new trend in engineering a novel function in naturally occurring hemoprotein.
Hayashi
Takashi
T
Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka 812-8581, Japan. thayatcm@mbox.nc.kyushu-u.ac.jp
Hisaeda
Yoshio
Y
D001665:Binding Sites; D006427:Hemin / Q000737:chemistry*; D008665:Metalloporphyrins / Q000737:chemistry; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry*; D009942:Organometallic Compounds; D011422:Propionates / Q000737:chemistry; D011487:Protein Conformation
D008665:Metalloporphyrins; D009211:Myoglobin; D009942:Organometallic Compounds; D011422:Propionates; D006427:Hemin