| | 1 | Author
| ElfriedeK. Pistorius | Requires cookie* | | | Title
| 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  | | | | Abstract
| The L-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 > 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~ > N 0 3_ > CL, Br > I~ > F ' > H CO O " > CH,COO . The inhibition of the L-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 L-amino acid oxidase activity and photosynthetic 0 2 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 0 2 evolution, we investigated whether a correlation could be obtained between the anion effect on the L-amino acid oxidase and on photosynthetic 0 2 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 0 2 evolu tion. Moreover, we show that L-arginine which is a substrate of the L-amino acid oxidase, and Cl-have antagonistic effects on the L-amino acid oxidase reaction and on photosynthetic 0 2 evolu tion. We suggest that this flavoprotein with L-amino acid oxidase activity is modified by Ca:+ and CL in such a way that it can now interact with Mn2* and catalyze the water-splitting reaction of photosystem II. | | | |
Reference
| Z. Naturforsch. 40c, 806—813 (1985); received June 7 1985 | | | |
Published
| 1985 | | | |
Keywords
| Anacystis nidulans, 0 2 Evolution, L-Amino Acid Oxidase, Chloride | | | |
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| default:Reihe_C/40/ZNC-1985-40c-0806.pdf | | | | Identifier
| ZNC-1985-40c-0806 | | | | Volume
| 40 | |
| 2 | Author
| Gudrun Wälzlein, AchimE. Gau, ElfriedeK. Pistorius | Requires cookie* | | | Title
| Further Investigations about the Flavin in the L-Amino Acid Oxidase and a Possible Flavin in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans | | | | Abstract
| The absorption spectrum of the previously purified L-amino acid oxidase from the cyanobac-terium Anacystis nidulans has shown considerable variation with each preparation and the spec-trum 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 L-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 L-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 L-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 photosys-tem 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. | | | |
Reference
| Z. Naturforsch. 43c, 545—553 (1988); received January 25 1988 | | | |
Published
| 1988 | | | |
Keywords
| L-Amino Acid Oxidase, Flavoprotein, Photosystem II, Cyanobacteria, Anacystis nidulans | | | |
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| default:Reihe_C/43/ZNC-1988-43c-0545.pdf | | | | Identifier
| ZNC-1988-43c-0545 | | | | Volume
| 43 | |
| 3 | Author
| AchimE. Gau, Gudrun Wälzlein, Susanne Gärtner, Matthias Kuhlmann, Susanne Specht, ElfriedeK. Pistorius | Requires cookie* | | | Title
| Immunological Identification of Polypeptides in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans | | | | 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 iden tification 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. | | | |
Reference
| Z. Naturforsch. 44c, 971—975 (1989); received June 22 1989 | | | |
Published
| 1989 | | | |
Keywords
| Photosystem II, L-Amino Acid Oxidase, Antibody, Cyanobacteria, Anacystis nidulans | | | |
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| default:Reihe_C/44/ZNC-1989-44c-0971.pdf | | | | Identifier
| ZNC-1989-44c-0971 | | | | Volume
| 44 | |
| 6 | Author
| Klaus-Peter Michel, ElfriedeK. Pistorius, E. Gau, G. Wälzlein, S. Gärtner, M. Kuhlmann, E. K. Pistorius | Requires cookie* | | | Title
| Isolation of a Photosystem II Associated 36 kDa Polypeptide and an Iron-Stress 34 kDa Polypeptide from Thylakoid Membranes of the Cyanobacterium Synechococcus PCC 6301 Grown under Mild Iron Deficiency | | | | Abstract
| A 36 kDa polypeptide which previously was shown to be present in purified photosystem II complexes from Synechococcus PCC 6301 and which crossreacts with the antiserum raised against the soluble L-amino acid oxidase o f 50 kD a from Synechococcus PCC 6301 (A. was isolated from thylakoid membranes o f the same cyanobacterium grown under mild iron deficiency. This peptide is present in about equal am ounts in thylakoid membranes o f Syne chococcus PCC 6301 grown under regular or iron deficient conditions. The antiserum raised against this thylakoid membrane bound 36 kD a peptide crossreacts with the soluble L-amino acid oxidase o f 50 kDa. These results further support our conclusion that the thylakoid mem brane bound 36 kD a polypeptide is a modified form o f the soluble 50 kD a L-amino acid oxi dase. In addition, a 34 kD a polypeptide was isolated from iron stressed thylakoid membranes, and an antiserum was also raised against this protein. Im m unoblot experiments with this an tiserum show that the 34 kD a peptide is present in elevated amounts in thylakoid membranes from Synechococcus cells grown under iron deficiency and that it is alm ost absent in thylakoid membranes from cells grown under regular conditions. | | | |
Reference
| Z. Naturforsch. 47c, 867—8 (1992); received August 4/O ctober 8 1992 | | | |
Published
| 1992 | | | |
Keywords
| Cyanobacteria, Synechococcus PCC 6301, Photosystem II, L-Amino Acid Oxidase, Iron Stress | | | |
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| default:Reihe_C/47/ZNC-1992-47c-0867.pdf | | | | Identifier
| ZNC-1992-47c-0867 | | | | Volume
| 47 | |
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