Enzymological Basis for Growth Inhibition by l -Phenylalanine in the Cyanobacterium Synechocystis sp. 29108
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چکیده
منابع مشابه
Iron reduction by the cyanobacterium Synechocystis sp. PCC 6803.
Synechocystis sp. PCC 6803 uptakes iron using a reductive mechanism, similar to that exhibited by many other microalgae. Various bio-electrochemical technologies have made use of this reductive cellular capacity, but there is still a lack of fundamental understanding of cellular reduction rates under different conditions. This study used electrochemical techniques to further investigate the red...
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Although methylated arsenic and arsenosugars have been verified in various freshwater organisms, lipidsoluble arsenic compounds have not been identified. Here, we report investigations with the model organism cyanobacterium Synechocystis sp. PCC 6803 wild type andDarsM (arsenic(III) S-adenosylmethionine methyltransferase) mutant strain, which lacks the enzymes for arsenic methylation cultured i...
متن کاملPhotokinesis of Cyanobacterium Synechocystis sp. PCC 6803
Motile cyanobacterium Synechocystis sp. PCC 6803 cells show photomovement with respect to the light stimulus. Under lateral irradiation, Synechocystis displays a phototactic gliding movement toward the light source by a twodimensional random biased walk. Under vertical irradiation, Synechocystis decreased the frequency of mean vectorial gliding speed dependent on the applied fluence rate, where...
متن کامل[NiFe]-hydrogenase is essential for cyanobacterium Synechocystis sp. PCC 6803 aerobic growth in the dark
The cyanobacterium Synechocystis sp. PCC 6803 has a bidirectional [NiFe]-hydrogenase (Hox hydrogenase) which reversibly reduces protons to H2. This enzyme is composed of a hydrogenase domain and a diaphorase moiety, which is distinctly homologous to the NADH input module of mitochondrial respiratory Complex I. Hox hydrogenase physiological function is still unclear, since it is not required for...
متن کاملThioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803.
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 e...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1980
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.144.3.1034-1042.1980