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JXB Advance Access originally published online on February 12, 2009
Journal of Experimental Botany 2009 60(3):1035-1046; doi:10.1093/jxb/ern352
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© 2009 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803

Sarah Schriek, Uwe Kahmann, Dorothee Staiger, Elfriede K. Pistorius and Klaus-Peter Michel*

Lehrstuhl für Molekulare Zellphysiologie, Universität Bielefeld, Universitätsstr. 25, D-33615 Bielefeld, Germany

* To whom correspondence should be addressed: E-mail: klauspeter.michel{at}uni-bielefeld.de

The protein Slr0782 from Synechocystis sp. PCC 6803, which has similarity to L-amino acid oxidase from Synechococcus elongatus PCC 6301 and PCC 7942, has been characterized in part. Immunoblot blot analysis showed that Slr0782 is mainly thylakoid membrane-associated. Moreover, expression of slr0782 mRNA and Slr0782 protein were analyzed and an activity assay was developed. Utilizing toluene-permeabilized cells, an L-arginine-stimulated O2 uptake became detectable in Synechocystis sp. PCC 6803. Besides oxidizing the basic L-amino acids L-arginine, L-lysine, L-ornithine, and L-histidine, a number of other L-amino acids were also substrates, while D-amino acids were not. The best substrate was L-cysteine, and the second best was L-arginine. The L-arginine-stimulated O2 uptake was inhibited by cations. The inhibition by o-phenanthroline and salicylhydroxamic acid suggested the presence of a transition metal besides FAD in the enzyme. Moreover, it is shown that inhibitors of the respiratory electron transport chain, such as KCN and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone, also inhibited the L-arginine-stimulated O2 uptake, suggesting that Slr0782 functions as an L-arginine dehydrogenase, mediating electron transfer from L-arginine into the respiratory electron transport chain utilizing O2 as electron acceptor via cytochrome oxidase. The results imply that Slr0782 is an additional substrate dehydrogenase being able to interact with the electron transport chain of the thylakoid membrane.

Key words: L-amino acid oxidase/dehydrogenase, L-arginine catabolism, Synechocystis sp. PCC 6803, electron transport chain

Received 23 October 2008; Revised 8 December 2008 Accepted 9 December 2008


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