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Thioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803
Author(s) -
Yamamoto Hiroshi,
Miyake Chikahiro,
Dietz Karl-Josef,
Tomizawa Ken-Ichi,
Murata Norio,
Yokota Akiho
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00309-9
Subject(s) - synechocystis , cyanobacteria , chemistry , biochemistry , peroxidase , enzyme , biology , bacteria , genetics
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 H 2 O 2 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 H 2 O 2 ‐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.