Redox properties of tyrosine and related molecules.
Redox reactions of tyrosine play key roles in many biological processes, including water oxidation and DNA synthesis. We first review the redox properties of tyrosine (and other phenols) in small molecules and related polypeptides, then report work on (H20)/(Y48)-modified Pseudomonas aeruginosa azurin. The crystal structure of this protein (1.18Å resolution) shows that H20 is strongly hydrogen bonded to Y48 (2.7-2.8Å tyrosine-O to histidine-N distance). A firm conclusion is that proper tuning of the tyrosine potential by a proton-accepting base is critical for biological redox functions.
Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA.
Jeffrey J
JJ
Warren
Jay R
JR
Winkler
Harry B
HB
Gray
D001400:Azurin / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D006639:Histidine / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000378:metabolism; D014443:Tyrosine / Q000737:chemistry* / Q000378:metabolism
D001400:Azurin; D014443:Tyrosine; D006639:Histidine