Structure and mechanism of copper, zinc superoxide dismutase.

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

Nature

journal_title

Nature

authors

Tainer JA,Getzoff ED,Richardson JS,Richardson DC

doi

10.1038/306284a0

subject

Has Abstract

pub_date

1983-11-17 00:00:00

pages

284-7

issue

5940

eissn

0028-0836

issn

1476-4687

journal_volume

306

pub_type

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