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Lumenal proteins involved in respiratory electron transport in the cyanobacterium Synechocystis sp. PCC6803

Lumenal proteins involved in respiratory electron transport in the cyanobacterium Synechocystis... Cyanobacterial thylakoids catalyze both photosynthetic and respiratory activities. In a photosystem I-less Synechocystis sp. PCC 6803 strain, electrons generated by photosystem II appear to be utilized by cytochrome oxidase. To identify the lumenal electron carriers (plastocyanin and/or cytochromes c 553, c 550, and possibly c M) that are involved in transfer of photosystem II-generated electrons to the terminal oxidase, deletion constructs for genes coding for these components were introduced into a photosystem I-less Synechocystis sp. PCC 6803 strain, and electron flow out of photosystem II was monitored in resulting strains through chlorophyll fluorescence yields. Loss of cytochrome c 553 or plastocyanin, but not of cytochrome c 550, decreased the rate of electron flow out of photosystem II. Surprisingly, cytochrome c M could not be deleted in a photosystem I-less background strain, and also a double-deletion mutant lacking both plastocyanin and cytochromec 553 could not be obtained. Cytochrome c M has some homology with the cytochrome c-binding regions of the cytochromecaa3 -type cytochrome oxidase from Bacillus spp. and Thermus thermophilus. We suggest that cytochrome c M is a component of cytochrome oxidase in cyanobacteria that serves as redox intermediate between soluble electron carriers and the cytochromeaa3 complex, and that either plastocyanin or cytochrome c 553 can shuttle electrons from the cytochrome b6f complex to cytochrome c M. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Lumenal proteins involved in respiratory electron transport in the cyanobacterium Synechocystis sp. PCC6803

Plant Molecular Biology , Volume 35 (4) – Sep 30, 2004

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References (32)

Publisher
Springer Journals
Copyright
Copyright © 1997 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
DOI
10.1023/A:1005875124387
Publisher site
See Article on Publisher Site

Abstract

Cyanobacterial thylakoids catalyze both photosynthetic and respiratory activities. In a photosystem I-less Synechocystis sp. PCC 6803 strain, electrons generated by photosystem II appear to be utilized by cytochrome oxidase. To identify the lumenal electron carriers (plastocyanin and/or cytochromes c 553, c 550, and possibly c M) that are involved in transfer of photosystem II-generated electrons to the terminal oxidase, deletion constructs for genes coding for these components were introduced into a photosystem I-less Synechocystis sp. PCC 6803 strain, and electron flow out of photosystem II was monitored in resulting strains through chlorophyll fluorescence yields. Loss of cytochrome c 553 or plastocyanin, but not of cytochrome c 550, decreased the rate of electron flow out of photosystem II. Surprisingly, cytochrome c M could not be deleted in a photosystem I-less background strain, and also a double-deletion mutant lacking both plastocyanin and cytochromec 553 could not be obtained. Cytochrome c M has some homology with the cytochrome c-binding regions of the cytochromecaa3 -type cytochrome oxidase from Bacillus spp. and Thermus thermophilus. We suggest that cytochrome c M is a component of cytochrome oxidase in cyanobacteria that serves as redox intermediate between soluble electron carriers and the cytochromeaa3 complex, and that either plastocyanin or cytochrome c 553 can shuttle electrons from the cytochrome b6f complex to cytochrome c M.

Journal

Plant Molecular BiologySpringer Journals

Published: Sep 30, 2004

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