Open AccessCytochrome c-553 is not required for photosynthetic activity in the cyanobacterium Synechococcus.
Author(s) -
David E. Laudenbach,
S. Herbert,
Cathy McDowell,
David C. Fork,
Arthur Grossman,
Neil A. Straus
Publication year - 1990
Publication title -
the plant cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.324
H-Index - 341
eISSN - 1532-298X
pISSN - 1040-4651
DOI - 10.1105/tpc.2.9.913
Subject(s) - cytochrome , cytochrome b6f complex , cytochrome c , biology , cytochrome f , cytochrome b , photosystem ii , biochemistry , cyanobacteria , mutant , synechococcus , photosynthesis , electron transport chain , photosystem i , coenzyme q – cytochrome c reductase , photosystem , gene , mitochondrion , bacteria , enzyme , mitochondrial dna , genetics
In cyanobacteria, the water-soluble cytochrome c-553 functions as a mobile carrier of electrons between the membrane-bound cytochrome b6-f complex and P-700 reaction centers of Photosystem I. The structural gene for cytochrome c-553 (designated cytA) of the cyanobacterium Synechococcus sp. PCC 7942 was cloned, and the deduced amino acid sequence was shown to be similar to known cyanobacterial cytochrome c-553 proteins. A deletion mutant was constructed that had no detectable cytochrome c-553 based on spectral analyses and tetramethylbenzidine-hydrogen peroxide staining of proteins resolved by polyacrylamide gel electrophoresis. The mutant strain was not impaired in overall photosynthetic activity. However, this mutant exhibited a decreased efficiency of cytochrome f oxidation. These results indicate that cytochrome c-553 is not an absolute requirement for reducing Photosystem I reaction centers in Synechococcus sp. PCC 7942.
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