The 1.6 A resolution structure of Fe-superoxide dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus.
The iron-containing superoxide dismutase (FeSOD) from the thermophilic cyanobacterium Thermosynechococcus elongatus has been isolated. The protein crystallizes readily and we have determined the structure to 1.6 A resolution. This is the first structural characterization of an FeSOD isolated from a cyanobacterium and one of the highest resolution FeSOD structures determined to date. The activity of the T. elongatus FeSOD has been measured both at 25 degrees C and 50 degrees C and it has been spectroscopically characterized. The T. elongatus FeSOD EPR spectra at pH 5.1, 7.5 and 10.0 are similar. This indicates that no change in the geometry of the Fe(III) site occurs over a wide range of pH. This is in contrast to the other FeSODs described in the literature.
Kerfeld
Cheryl A
CA
Molecular Biology Institute, UCLA, Box 951570, Los Angeles, CA 90095-1570, USA.
Yoshida
Stephanie
S
Tran
Kimberlee T
KT
Yeates
Todd O
TO
Cascio
Duilio
D
Bottin
Hervé
H
Berthomieu
Catherine
C
Sugiura
Miwa
M
Boussac
Alain
A
D001426:Bacterial Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D016415:Sequence Alignment; D013482:Superoxide Dismutase / Q000737:chemistry*; D013696:Temperature
D001426:Bacterial Proteins; D013482:Superoxide Dismutase