Abstract:
:Copper, zinc superoxide dismutase (SOD) catalyses the very rapid two-step dismutation of the toxic superoxide radical (O-2) to molecular oxygen and hydrogen peroxide through the alternate reduction and oxidation of the active-site copper. We report here that after refitting and further refinement of the previous 2 A structure of SOD2, analysis of the new model and its calculated molecular surface shows an extensive surface topography of sequence-conserved residues stabilized by underlying tight packing and H-bonding. There is a single, highly complementary position for O-2 to bind to both the Cu(II) and activity-important Arg 141 with correct geometry; two water molecules form a ghost of the superoxide in this position. The geometry and molecular surface of the active site, together with biochemical data, suggest a specific model for the enzyme mechanism.
journal_name
Naturejournal_title
Natureauthors
Tainer JA,Getzoff ED,Richardson JS,Richardson DCdoi
10.1038/306284a0subject
Has Abstractpub_date
1983-11-17 00:00:00pages
284-7issue
5940eissn
0028-0836issn
1476-4687journal_volume
306pub_type
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