Isolation And Partial Characterization Of An L -Amino Acid Oxidase And Of Photosystem Ii Complexes From The Cyanobacterium Synechococcus PCC7942

Engels, Dirk H.; Engels, Anke; Pistorius, Elfriede K.

doi:10.1515/znc-1992-11-1212

Cited by 12 publications

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“…Immunocytochemical detection of the l-amino acid oxidase in Synechococcus elongatus PCC 7942. Immunocytochemical detection of the l-Aox (encoded by the aoxA) with the anti-l-Aox antiserum (Engels et al, 1992) in combination with gold-labeled anti-rabbit IgG. The cells were grown in BG11 medium for 3 days.…”

Section: Resultsmentioning

confidence: 99%

“…Growth and French press extract preparation were as described in Yousef et al (2003). The l-Aox activity was determined as described in Engels et al (1992), and the immunocytochemical investigation was done as described in Bockholt et al (1996) utilizing the antiserum raised against the isolated l-Aox from Synechococcus elongatus PCC 6301.…”

Section: Methodsmentioning

confidence: 99%

“…Previously, we have shown that the l-Aox from Synechococcus elongatus PCC 6301 as well as from PCC 7942 contain noncovalently bound FAD as a prosthetic group (Pistorius and Voss, 1980;Engels et al, 1992). The peptide fragment between amino acid residues 42 to 70 in Synechococcus elongatus PCC 6301 contains the highly conserved motif of a dinucleotide binding site according to Wierenga et al (1986) (Fig.…”

Section: Characteristics Of the Fad-binding Motifmentioning

confidence: 98%

“…Therefore, the function of these enzymes in the overall metabolisms of the cyanobacteria is of interest and is presently still unknown. It is well documented that the isolated l-Aox (encoded by the aoxA) of Synechococcus elongatus PCC 6301 and PCC 7942 as well as Synechococcus cedrorum PCC 6908 catalyzes the oxidative deamination of basic l-amino acids with larginine as best substrate (Pistorius and Voss, 1980;Engels et al, 1992; Table II). Since the enzyme is in part located extracellularly, a role in utilizing extracellular larginine as N-source in natural environments could be assumed.…”

Section: Evaluating Of 24 Cyanobacterial Genome Sequences For the Prementioning

confidence: 99%

“…The two closely related cyanobacteria Synechococcus elongatus PCC 6301 and Synechococcus elongatus PCC 7942 have previously been shown to possess a FAD-containing l-amino acid oxidase (l-Aox) catalyzing the oxidative deamination of basic l-amino acids (l-Arg Ͼ l-Lys Ͼ l-Orn Ͼ lHis) by utilizing O 2 as electron acceptor resulting in the formation of the corresponding ketoacid, ammonium, and hydrogen peroxide (Pistorius et al, 1979;Pistorius and Voss, 1980;Engels et al, 1992). Another rather unusual property, besides having a high specificity for basic l-amino acids, is its strong inhibition by cations (M 3+ Ͼ M 2+ Ͼ M + ) and less strong inhibition by anions.…”

Section: Introductionmentioning

confidence: 99%

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L-Amino Acid Oxidases with Specificity for Basic L-Amino Acids in Cyanobacteria

Gau

Heindl

Nodop

et al. 2007

Zeitschrift Für Naturforschung C

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The two closely related fresh water cyanobacteria Synechococcus elongatus PCC 6301 and Synechococcus elongatus PCC 7942 have previously been shown to constitutively express a FAD-containing l-amino acid oxidase with high specificity for basic l-amino acids (l-arginine being the best substrate). In this paper we show that such an enzyme is also present in the fresh water cyanobacterium Synechococcus cedrorum PCC 6908. In addition, an improved evaluation of the nucleotide/amino acid sequence of the l-amino acid oxidase of Synechococcus elongatus PCC 6301 (encoded by the aoxA gene) with respect to the FAD-binding site and a translocation pathway signal sequence will be given. Moreover, the genome sequences of 24 cyanobacteria will be evaluated for the occurrence of an aoxA-similar gene. In the evaluated cyanobacteria 15 genes encoding an l-amino acid oxidase-similar protein will be found.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Characteristics Of the Fad-binding Motifmentioning

confidence: 98%

Section: Evaluating Of 24 Cyanobacterial Genome Sequences For the Prementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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L-Amino Acid Oxidases with Specificity for Basic L-Amino Acids in Cyanobacteria

Gau

Heindl

Nodop

et al. 2007

Zeitschrift Für Naturforschung C

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Inactivation of the water-oxidizing enzyme in manganese stabilizing protein-free mutant cells of the cyanobacteria Synechococcus PCC7942 and Synechocystic PCC6803 during dark incubation and conditions leading to photoactivation

et al. 1994

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The previously constructed MSP (manganese stabilizing protein-psbO gene product)-free mutant of Synechococcus PCC7942 (Bockholt R, Masepohl B and Pistorius E K (1991) FEBS Lett 294: 59-63) and a newly constructed MSP-free mutant of Synechocystis PCC6803 were investigated with respect to the inactivation of the water-oxidizing enzyme during dark incubation. O2 evolution in the MSP-free mutant cells, when measured with a sequence of short saturating light flashes, was practically zero after an extended dark adaptation, while O2 evolution in the corresponding wild type cells remained nearly constant. It could be shown that this inactivation could be reversed by photoactivation. With isolated thylakoid membranes from the MSP-free mutant of PCC7942, it could be demonstrated that photoactivation required illumination in the presence of Mn(2+) and Ca(2+), while Cl(-) addition was not required under our experimental conditions. Moreover, an extended analysis of the kinetic properties of the water-oxidizing enzyme (kinetics of the S3→(S4)→S0 transition, S-state distribution, deactivation kinetics) in wild type and mutant cells of Synechococcus PCC7942 and Synechocystis PCC6803 was performed, and the events possibly leading to the reversible inactivation of the water-oxidizing enzyme in the mutant cells are discussed. We could also show that the water-oxidizing enzyme in the MSP-free mutant cells is more sensitive to inhibition by added NH4Cl-suggesting that NH3 might be a physiological inhibitor of the water oxidizing enzyme in the absence of MSP.

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New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942

et al. 2011

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Iron limitation has a strong impact on electron transport reactions of the unicellular fresh water cyanobacterium Synechococcus elongatus PCC 7942 (thereafter referred to as S. elongatus). Among the various adaptational processes on different cellular levels, iron limitation induces a strongly enhanced expression of IdiC (iron-deficiency-induced protein C). In this article, we show that IdiC is loosely attached to the thylakoid and to the cytoplasmic membranes and that its expression is enhanced during conditions of iron starvation and during the late growth phase. The intracellular IdiC level was even more increased when additional iron was replenished in the late growth phase. On the basis of its amino acid sequence and of its absorbance spectrum, IdiC can be classified as a member of the family of thioredoxin (TRX)-like (2Fe-2S) ferredoxins. The presence of an iron cofactor in IdiC was detected by inductive coupled plasma optical emission spectrometry (ICP-OES). Comparative measurements of electron transport activities of S. elongatus wild type (WT) and an IdiC-merodiploid mutant called MuD, which contained a strongly reduced IdiC content under iron-sufficient as well as iron-deficient growth conditions, were performed. The results revealed that MuD had a strongly increased light sensitivity, especially under iron limitation. The measurements of photosystem II (PS II)-mediated electron transport rates in WT and MuD strain showed that PS II activity was significantly lower in MuD than in the WT strain. Moreover, P(700) (+) re-reduction rates provided evidence that the respiratory activities, which were very low in the MuD strain in the presence of iron, significantly increased in iron-starved cells. Thus, an increase in respiration may compensate for the drastic decrease of photosynthetic electron transport activity in MuD grown under iron starvation. Based on the similarity of the S. elongatus IdiC to the NuoE subunit of the NDH-1 complex in Escherichia coli, it is likely that IdiC has a function in the electron transport processes from NAD(P)H to the plastoquinone pool. This is in agreement with the up-regulation of IdiC in the late growth phase as well as under stress conditions when PS II is damaged. As absence or high reduction of the IdiC level would prevent or reduce the formation of functional NDH-1 complexes, under such conditions electron transport routes via alternative substrate dehydrogenases, donating electrons to the plastoquinone pool, can be assumed to be up-regulated.

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Isolation And Partial Characterization Of An L -Amino Acid Oxidase And Of Photosystem Ii Complexes From The Cyanobacterium Synechococcus PCC7942

Cited by 12 publications

References 0 publications

L-Amino Acid Oxidases with Specificity for Basic L-Amino Acids in Cyanobacteria

L-Amino Acid Oxidases with Specificity for Basic L-Amino Acids in Cyanobacteria

Inactivation of the water-oxidizing enzyme in manganese stabilizing protein-free mutant cells of the cyanobacteria Synechococcus PCC7942 and Synechocystic PCC6803 during dark incubation and conditions leading to photoactivation

New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942

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