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Conservation of local electric fields in the evolution of Cu,Zn superoxide dismutase
Author(s) -
Desideri Alessandro,
Falconi Mattia,
Parisi Valerio,
Rotilio Giuseppe
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80681-7
Subject(s) - electric field , superoxide dismutase , substrate (aquarium) , chemistry , flux (metallurgy) , enzyme , superoxide , active site , chemical physics , catalysis , analytical chemistry (journal) , biophysics , biochemistry , biology , ecology , physics , environmental chemistry , organic chemistry , quantum mechanics
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.