Conservation of local electric fields in the evolution of Cu,Zn superoxide dismutase.
The trend of the electric field and the value of the electric field flux, sensed by the superoxide substrate in the proximity of the active site, were found to be constant in three highly homologous Cu,Zn superoxide dismutases from ox, pig and sheep, which display large differences in net protein charge and distribution of electrically charged surface residues but very similar catalytic rate constants. The spatial relationship of charges on the protein surface apparently has been conserved during the evolution of this enzyme to create electrostatic facilitation of catalysis.
Desideri
A
A
Department of Biology, Tor Vergata University of Rome, Italy.
Falconi
M
M
Parisi
V
V
Rotilio
G
G
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D002417:Cattle; D004563:Electrochemistry; D007700:Kinetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012756:Sheep; D013482:Superoxide Dismutase / Q000235:genetics* / Q000378:metabolism; D013552:Swine
D013482:Superoxide Dismutase