Presence of an Amino Acid Oxidase in O2 Evolving Photosystem II Preparations from the Cyanobacterium Anacystis nidulans

1987 ◽  
pp. 185-186
Author(s):  
E. K. Pistorius ◽  
A. E. Gau
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Anacystis Nidulans ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

scholarly journals Presence of an Amino Acid Oxidase in Photosystem II of Anacystis nidulans

1982 ◽  
Vol 126 (1) ◽  
pp. 203-209 ◽  
Author(s):  
Elfriede K. PISTORIUS ◽  
Helga VOSS
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Anacystis Nidulans ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

Further Evidence for a Functional Relationship between L-Amino Acid Oxidase Activity and Photosynthetic Oxygen Evolution in Anacystis nidulans. Effect of Chloride on the Two Reactions

1985 ◽  
Vol 40 (11-12) ◽  
pp. 806-813 ◽  
Author(s):  
Elfriede K. Pistorius
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Water Splitting ◽  
Oxidase Activity ◽  
Functional Relationship ◽  
Anacystis Nidulans ◽  
Acid Oxidase ◽  
Photosynthetic Oxygen Evolution ◽  
Amino Acid Oxidase ◽  
Oxidase Reaction

Abstract The ʟ-amino acid oxidase from Anacystis nidulans is inhibited by cations as well as anions. The inhibition by cations has been previously described (E. K. Pistorius, Eur. J. Biochem. 135, 217-222 [1983]). We have shown that the order of effectiveness was M3+ > M2+ > M+, when e.g. La3+, Ca2+ and K+ were compared. However, in the concentration range where the monovalent cations inhibited, the inhibition was not entirely due to the cation, but an influence of the anion could also be observed. When monovalent anions were compared as the corresponding sodium salts, the order of effectiveness was SCN- > NO3- > CL-, Br- > I- > F- > HCOO- > CH3COO- . The inhibition of the ʟ-amino acid oxidase activity by the various salts was strongly influenced by the pH of the reaction mixture. It could be shown that the inhibition by cations increased in the alkaline pH region, while the inhibition by anions increased in the acidic pH region.Our previous results have also shown that a functional relationship might exist between ʟ-amino acid oxidase activity and photosynthetic O2 evolution (E. K. Pistorius and H. Voss, Eur. J. Biochem. 126, 203-209 [1982]). Since the water-splitting complex of photosystem II is affected by a number of anions, although only Cl- and Br- lead to activation of O2 evolution, we investigated whether a correlation could be obtained between the anion effect on the ʟ-amino acid oxidase and on photosynthetic O2 evolution. The results show that those anions which have a higher affinity for the enzyme than CL- or Br-, are especially effective in causing inactivation of the O2 evolution. Moreover, we show that ʟ-arginine which is a substrate of the ʟ-amino acid oxidase, and Cl- have antagonistic effects on the ʟ-amino acid oxidase reaction and on photosynthetic O2 evolution. We suggest that this flavoprotein with ʟ-amino acid oxidase activity is modified by Ca2+ and CL- in such a way that it can now interact with Mn2+ and catalyze the water-splitting reaction of photosystem II.

Investigations about various Possible Functions of the L -Amino Acid Oxidase in the Cyanobacterium Anacystis nidulans

1989 ◽  
Vol 44 (5-6) ◽  
pp. 370-377 ◽  
Author(s):  
Elfriede K. Pistorius ◽  
Regine Kertsch ◽  
Susanne Faby
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Divalent Cation ◽  
Anacystis Nidulans ◽  
Acid Oxidase ◽  
Sole Nitrogen Source ◽  
Amino Acid Oxidase ◽  
Cation Concentration ◽  
Arginine Catabolism ◽  
Photosystem Ii Activity

Abstract The cyanobacterium A nacystis nidulans was grown on nitrate or L-arginine as sole nitrogen source and in the presence of different divalent cation concentrations (1 mᴍ MgSO4 and 0.1 mᴍ CaCl2 or 0.1 mᴍ MgSO4 and 0.05 mᴍ CaCl2). The L-amino acid oxidase previously reported to be present in Anacystis nidulans (E . K. Pistorius and A. E. Gau, Biochim. Biophys. Acta 849, 203, 1986) was shown to be involved in L-arginine catabolism in cells grown with the lower divalentcation concentration. Under these conditions L-arginine was partly degraded via 2-ketoarginine and 4-guanidinobutyrate. On the other hand, at higher cation concentrations the ʟ-amino acid oxidase activity seem ed to be not sufficient to provide enough NH4+ from ʟ-arginine for cell growth. Under those conditions photosystem II activity was initially reduced, and growth on ʟ-arginine could only start after photosystem II activity increased again and after arginase was induced. The arginase pathway was functional in A . nidulans grown on ʟ-arginine independently of the divalent cation concentration in the medium. A tentative scheme of the various functiona roles of the ʟ-amino acid oxidase protein in A . nidulans is given. This model combines the here presented and the previous results and suggests that the ʟ-amino acid oxidase is functional in photosynthetic and respiratory activities as well as in ʟ-arginine degradation in A . nidulans. All these activities of the ʟ-amino acid oxidase protein are greatly influenced by the divalent cation concentration in the growth medium.

Immunological Identification of Polypeptides in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans

1989 ◽  
Vol 44 (11-12) ◽  
pp. 971-975 ◽  
Author(s):  
Achim E. Gau ◽  
Gudrun Wälzlein ◽  
Susanne Gärtner ◽  
Matthias Kuhlmann ◽  
Susanne Specht ◽  
...  
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Gradient Centrifugation ◽  
Anacystis Nidulans ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Western Blots ◽  
Ps Ii ◽  
Processed Form ◽  
Coomassie Brilliant

Abstract Photosystem II complexes from the cyanobacterium Anacystis nidulans have been investigated by Western blots with antisera raised against four photosystem II peptides from plants and with an antiserum raised against the soluble L-amino acid oxidase protein from/1. nidulans to achieve an iden­tification of the polypeptides - especially of the L-amino acid oxidase related protein - in isolated photosystem II complexes. Anacystis photosystem II complexes which were solubilized with lauryldimethylamine N-oxide and purified by sucrose cushion and sucrose gradient centrifugation, contained as major Coomassie brilliant blue stained polypeptides a 71 kDa band of unknown identity, a 62 kDa band, which partly contained D-l, a 55 and 49 kDa band which were immuno-reactive with an antiserum to the 47 kDa peptide of tobacco PS II complexes, and three distinct bands in the 30 kDa region. These latter bands could be identified as the extrinsic Mn stabilizing peptide (27-30 kDa), D-l (30-33 kDa) and a 36 kDa peptide (35 - 38 kDa) which crossreacted with the antiserum raised against the soluble L-amino acid oxidase protein of 50 kDa. These results suggest that the 36 kDa peptide present in purified photosystem II complexes from A. nidulans might be a processed form of the soluble 50 kDa L-amino acid oxidase protein.

Further Investigations about the Flavin in the L-Amino Acid Oxidase and a Possible Flavin in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans

1988 ◽  
Vol 43 (7-8) ◽  
pp. 545-553 ◽  
Author(s):  
Gudrun Wälzlein ◽  
Achim E. Gau ◽  
Elfriede K. Pistorius
Keyword(s):  
Absorption Spectrum ◽  
Amino Acid ◽  
Photosystem Ii ◽  
Fluorescence Emission ◽  
Anacystis Nidulans ◽  
Acid Oxidase ◽  
Donor Side ◽  
Amino Acid Oxidase ◽  
Unknown Structure ◽  
Additional Support

The absorption spectrum of the previously purified ʟ-amino acid oxidase from the cyanobacterium Anacystis nidulans has shown considerable variation with each preparation and the spectrum in several preparations was quite different from the absorption spectrum of other simple flavoproteins (E. K. Pistorius and A. E. Gau, Biochim. Biophys. Acta 849, 203, 1986). Here we show that the spectral complexity and variability of the ʟ-amino acid oxidase can be largely explained by the presence of a modified flavin derivative of yet unknown structure besides oxidized FAD and FAD semiquinone. After removal from the enzyme this modified chromophore has absorption maxima at 260, 396 and in the 600 nm region. This derivative of FAD seems to be formed in variable amounts during the purification of the enzyme. On the other hand, extraction of Anacystis photosystem II complexes which contain the flavoprotein, almost exclusively yields modified flavin derivatives and practically no authentic oxidized FAD. The spectrum of the chromophores which have been extracted from photosystem II complexes at different purification stages, is either similar (although not identical) to the spectrum of the chromophore extracted from the isolated ʟ-amino acid oxidase or similar to the spectrum of reduced flavin. All extracted chromophores show a fluorescence emission in the 420 to 560 nm region when excited with light of 390 nm. These results indicate that the flavin present in the ʟ-amino acid oxidase protein as well as in photosystem II complexes from A. nidulans rapidly undergoes modification reactions of yet unknown nature to yield several closely related FAD derivatives. This might possibly be the reason why so far no flavin has been detected in photosystem II. The presence of such modified flavin derivatives in photosystem II complexes of A. nidulans as shown here is an additional support of our hypothesis that an unusual flavin is functional on the donor side of photosystem II.

Some properties of a basic l-amino-acid oxidase from Anacystis nidulans

1980 ◽  
Vol 611 (2) ◽  
pp. 227-240 ◽  
Author(s):  
Elfriede K. Pistorius ◽  
Helga Voss
Keyword(s):  
Amino Acid ◽  
Anacystis Nidulans ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

The Biosynthesis of Phenylacetic Acids in the Blue-Green Alga Anacystis nidulans: Evidence for the Involvement of a Thylakoid-Bound ʟ-Amino Acid Oxidase

1977 ◽  
Vol 32 (5-6) ◽  
pp. 345-350 ◽  
Author(s):  
W. Löffelhardt
Keyword(s):  
Amino Acid ◽  
Phenylacetic Acid ◽  
Higher Plants ◽  
Aromatic Amino Acids ◽  
Anacystis Nidulans ◽  
Acid Oxidase ◽  
Reaction Sequence ◽  
Amino Acid Oxidase ◽  
Blue Green Algae ◽  
Hydroxyphenylacetic Acid

Abstract Phenylacetic acid and p-hydroxyphenylacetic acid are formed upon incubation of photosynthetic membranes from the prokaryotic alga Anacystis nidulans with ʟ-phenylalanine and ʟ-tyrosine, respectively. The corresponding phenylpyruvic acids act as intermediates as shown by trapping them as the stable oximino acids. The first step in this reaction sequence appears to be catalyzed by a thylakoid-bound ʟ-amino acid oxidase. Already existing evidence concerning phenylacetic acid formation at thylakoid membranes of higher plants via an ʟ-amino acid oxidase and the results obtained with A. nidulans give another example of aromatic amino acids between chloroplasts and blue-green algae.

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