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FEBS Lett. 1999 Mar 26;447(2-3):269-73.

Thioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803.

Author information

1
Plant Molecular Physiology Laboratory, Research Institute of Innovative Technology for the Earth, Kizu, Kyoto, Japan.

Abstract

The amino acid sequence deduced from the open reading frame designated sll0755 in Synechocystis sp. PCC 6803 is similar to the amino acid sequences of thioredoxin peroxidases from other organisms. In the present study, we found that a recombinant SLL0755 protein that was expressed in Escherichia coli was able to reduce H2O2 and tertiary butyl hydroperoxide with thioredoxin from E. coli as the electron donor. Targeted disruption of open reading frame sll0755 in Synechocystis sp. PCC 6803 cells completely eliminated the H2O2-dependent and tertiary butyl hydroperoxide-dependent photosynthetic evolution of oxygen and the electron flow in photosystem II. These results indicate that the product of open reading frame sll0755 is a thioredoxin peroxidase whose activities are coupled to the photosynthetic electron transport system in Synechocystis sp. PCC 6803.

PMID:
10214959
DOI:
10.1016/s0014-5793(99)00309-9
[Indexed for MEDLINE]
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