J Biol Inorg Chem. 2003 Sep;8(7):707-14. Epub 2003 Jun 24.

The 1.6 A resolution structure of Fe-superoxide dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus.

Kerfeld CA, Yoshida S, Tran KT, Yeates TO, Cascio D, Bottin H, Berthomieu C, Sugiura M, Boussac A.

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Molecular Biology Institute, UCLA, Box 951570, Los Angeles, CA 90095-1570, USA.

Abstract

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.

PMID:: 12827458; [PubMed - indexed for MEDLINE]

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Structures reported by this article

The 1.6 A Structure Of Fe-Superoxide Dismutase From The Thermophilic Cyanobacterium Thermosynechococcus Elongatus : Correlation Of Epr And Structural Characteristics

PDB: 1MY6

Source: Thermosynechococcus elongatus

Method: X-Ray Diffraction

Resolution: 1.6 Å

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