Shall we dance? How a multicopper oxidase chooses its electron transfer partner.
Multicopper oxidases (MCOs) are encoded in the genomes of Eukarya, Bacteria, and Archea. These proteins are unique in that they contain at least four Cu atom prosthetic groups organized into one each of the three spectral classifications of copper sites in biology: type 1 (T1), type 2 (T2), and binuclear type 3 (T3), where the T2 and T3 sites form a trinuclear Cu cluster. With these four redox-active copper sites, the multicopper oxidases catalyze the four-electron (4e(-)) reduction of dioxygen to 2H2O, an activity that they alone share with the terminal heme-containing oxidases. Most MCOs exhibit broad specificity towards organic reductants, while a relatively small number of family members exhibit equally robust activity towards metal ions like Fe(II), Cu(I), and Mn(II) and, thus, are considered metallo-oxidases. This Account analyzes the structure-activity features of multicopper oxidases that determine their relative substrate specificity. Since the substrate oxidation step involves an outer-sphere electron transfer from the reductant to the T1Cu site in the protein, the concepts of Marcus theory are applied to unravel the origin of the substrate specificity of the multicopper ferroxidases.
Quintanar
Liliana
L
Centro de Investigación y de Estudios Avanzados, México, D.F., México.
Stoj
Christopher
C
Taylor
Alexander B
AB
Hart
P John
PJ
Kosman
Daniel J
DJ
Solomon
Edward I
EI
D001426:Bacterial Proteins / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D008667:Metalloproteins / Q000737:chemistry*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D008667:Metalloproteins; D003300:Copper; D010088:Oxidoreductases