| Literature DB >> 12827458 |
Cheryl A Kerfeld1, Stephanie Yoshida, Kimberlee T Tran, Todd O Yeates, Duilio Cascio, Hervé Bottin, Catherine Berthomieu, Miwa Sugiura, Alain Boussac.
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.Entities:
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Year: 2003 PMID: 12827458 DOI: 10.1007/s00775-003-0469-0
Source DB: PubMed Journal: J Biol Inorg Chem ISSN: 0949-8257 Impact factor: 3.358