The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins.
The crystal structure of catechol oxidase reveals new insight into the functional properties of the type-3 copper proteins. This class of proteins includes the closely related and better-known tyrosinase as well as hemocyanin, an oxygen transport protein. All these proteins have a dinuclear copper center, have similar spectroscopic behaviors, and show close evolutionary and functional relationships. Comparison between the 3D structures of catechol oxidase and hemocyanins reveals the structural reasons for the divergence in function.
Gerdemann
Carsten
C
Institut für Anorganische und Analytische Chemie der Universität Münster, Wilhelm-Klemm-Strasse 8, 48149 Münster, Germany.
Eicken
Christoph
C
Krebs
Bernt
B
D000595:Amino Acid Sequence; D004156:Catechol Oxidase / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D003300:Copper / Q000737:chemistry*; D003460:Crystallization; D006433:Hemocyanins / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D011487:Protein Conformation; D016415:Sequence Alignment; D013329:Structure-Activity Relationship
D008667:Metalloproteins; D010940:Plant Proteins; D003300:Copper; D006433:Hemocyanins; D004156:Catechol Oxidase