Ferredoxin aus Bumilleriopsis filiformis Vischer (original) (raw)
Literatur
Arnon, D. I.: Photosynthetic phosphorylation: Facts and concepts. In: Biochemistry of chloroplasts, vol. 2, 461–503, Hrsg. T. W. Goodwin. London-New York: Academic Press 1967. Google Scholar
Bachmayer, H., Piette, L. H., Yasunobu, K. T., Whiteley, H. R.: The binding site of iron in rubredoxin from Micrococcus aerogenes. Proc. nat. Acad. Sci. (Wash.) 57, 122–127 (1968). Google Scholar
—, Yasunobu, K. T., Whiteley, H. R.: The chelate structure of Micrococcus aerogenes rubredoxin. Proc. nat. Acad. Sci. (Wash.) 59, 1273–1277 (1968). Google Scholar
Bayer, E., Hagenmaier, H.: Structure and reconstitution of plant ferredoxin. In: Progress in photosynthesis research, vol. 3, p. 1427–1432, Hrsg. H. Metzner. Tübingen: H. Metzner 1969. Google Scholar
—, Josef, D., Krauss, P., Hagenmaier, R., Röder, A., Trebst, A.: Abbau und Resynthese these des Aktivzentrums vom Pflanzenferredoxin. Biochim. biophys. Acta (Amst.) 143, 435–437 (1967). Google Scholar
Beinert, H.: EPR Spectroscopy in the detection, study, and identification of protein-bound non-heme iron. In: Non-heme iron proteins, p. 23–42, Hrsg. A. San Pietro. Yellow Springs/Ohio: The Antioch Press 1965. Google Scholar
Beinert, H., Dervartanian, D. V., Hemmerich, P., Veeger, C., van Voorst, J. D. W.: On the Ligand field of redox active non-heme iron in proteins. Biochim. biophys. Acta (Amst.) 96, 530–533 (1965). Google Scholar
Bendall, D. S., Gregory, R. P. F., Hill, R.: Chloroplast ferredoxin from parsley. Biochem. J. 88, 29P-30P (1963). Google Scholar
Benson, A. M., Yasunobu, K. T.: Non-heme iron proteins. X. The amino acid sequence of ferredoxins from Leucaena glauca. J. biol. Chem. 244, 955–963 (1969). Google Scholar
Böger, P.: Photophosphorylierung mit Chloroplasten aus Bumilleriopsis filiformis Vischer. Z. Pflanzenphysiol. 61, 85–97 (1969a). Google Scholar
—: Ferredoxin-katalysierte Reaktionen im zellfreien System der Alge Bumilleriopsis filiformis Vischer. Z. Pflanzenphysiol. 61, 447–461 (1969b) Google Scholar
—: Algae preparations-phosphorylating. In: Methods in enzymology, vol. “Photosynthesis” London-New York: Academic Press 1970 (im Druck). Google Scholar
—, Black, C. C., San Pietro, A.: Photosynthetic reactions with pyridine nucleotide analogs. Arch. Biochem. 115, 35–43 (1966). Google Scholar
—, San Pietro, A.: Ferredoxin and cytochrome f in Euglena gracilis. Z. Pflanzenphysiol. 58, 70–75 (1967). Google Scholar
Bothe, H.: Ferredoxin und Phytoflavin in photosynthetischen Reaktionen einer Präparation aus der Blaualge Anacystis nidulans. Diss. Göttingen 1968.
Brintzinger, H., Palmer, G., Sands, R. H.: On the Ligand field of iron in ferredoxin from spinach chloroplasts and related non-heme iron enzymes. Proc. nat. Acad. Sci. (Wash.) 55, 397–404 (1966). Google Scholar
Buchanan, B., Kalberer, P. P., Arnon, D. I.: Ferredoxin-activated fructose diphosphatase in isolated chloroplasts. Biochem. biophys. Res. Commun. 29, 74–79 (1967). Google Scholar
Cooke, R., Tsibris, J. C. M., Debrunner, P. G., Tsai, R., Gunsalus, I. C., Frauenfelder, H.: Mössbauer studies on putidaredoxin. Proc. nat. Acad. Sci. (Wash.) 59, 1045–1052 (1968). Google Scholar
Davenport, H. E.: The role of soluble protein factors in chloroplast electron transport. In: Non-heme iron proteins, p. 115–135, Hrsg. A. San Pietro. Yellow Springs/Ohio: The Antioch Press 1965. Google Scholar
Ellman, G. L.: Tissue sulfhydryl groups. Arch. Biochem. 82, 70–77 (1959). PubMed Google Scholar
Evans, M. C. W., Hall, D. O., Bothe, H., Whatley, F. R.: The stoicheiometry of electron transfer by bacterial and plant ferredoxins. Biochem. J. 110, 485–489 (1968). Google Scholar
Fogo, J. K., Popowsky, M.: Spectrophotometric determination of hydrogen sulfide. Analyt. Chem. 21, 732–737 (1949). Google Scholar
Fry, K. T., Lazzarini, R., San Pietro, A.: The photoreduction of iron in photosynthetic pyridine nucleotide reductase. Proc. nat. Acad. Sci. (Wash.) 50, 652–657 (1963). Google Scholar
—, San Pietro, A.: Photosynthetic pyridine nucleotide reductase. IV. Further studies on the chemical properties of the protein. In: Photosynthetic mechanisms in green plants, p. 252–261, Hrsg. B. Kok u. A. T. Jagendorf. Washington D. C.: Natl. Research Council 1963. Google Scholar
Gerhardt, B., Trebst, A.: Photosynthetische Reaktionen in lyophylisierten Zellen der Blaualge Anacystis. Z. Naturforsch. 20b, 879–885 (1965). Google Scholar
Gillard, R. D., Mason, R., Mayhew, G. G., Peel, J. L., Stangroom, J. E.: Some effects of metal-binding agents on bacterial ferredoxin. In: Protides of the biological fluids, vol. 14, p. 159–163, Hrsg. H. Peeters. Amsterdam: Elsevier 1966. Google Scholar
—, McKenzie, E. D., Mason, R., Mayhew, S. G., Peel, J. L., Stangroom, J. E.: Nature of the non-heme iron in ferredoxin and rubredoxin. Nature (Lond.) 208, 769–771 (1965). Google Scholar
Hill, R., San Pietro, A.: Hydrogen transport with chloroplasts. Z. Naturforsch. 18b, 677–682 (1963). Google Scholar
Hong, J., Rabinowitz, J. C.: Preparation and properties of clostridial ferredoxin. Biochem. Biophys. Res. Commun. 29, 246–252 (1967). Google Scholar
Johnson, C. E., Elstner, E., Gibson, J. F., Benfield, G., Evans, M. G. W., Hall, D. O.: Mössbauer effect in the ferredoxin of Euglena. Nature (Lond.) 220, 1291–1293 (1968). Google Scholar
Katoh, S., Takamiya, A.: The iron-binding in photosynthetic pyridine nucleotide reductase. Arch. Biochem. 102, 189–200 (1963). Google Scholar
Keister, D. L., San Pietro, A., Stolzenbach, F. E.: Pyridine Nucleotide transhydrogenase from spinach. Biochem. biophys. Res. Commun. 1, 110–114 (1959). Google Scholar
———: Pyridine nucleotide transhydrogenase from spinach. II. Requirement of enzyme for photochemical accumulation of reduced pyridine nucleotides. Arch. Biochem. 98, 235–244 (1960). Google Scholar
Keresztes-Nagy, S., Margoliash, E.: Preparation and characterization of Alfalfa ferredoxin. J. biol. Chem. 241, 5955–5966 (1966). Google Scholar
Lovenberg, W., Buchanan, B. B., Rabinowitz, J. C.: Studies on the chemical nature of clostridial ferredoxin. J. biol. Chem. 238, 3899–3913 (1963). Google Scholar
Malkin, R., Rabinowitz, J. C.: Nonheme iron electron-transfer proteins. Ann. Rev. Biochem. 35, 113–148 (1966a). Google Scholar
——: The reconstitution of clostridial ferredoxin. Biochem. biophys. Res. Commun. 23, 822–827 (1966b). Google Scholar
——: The reactivity of clostridial ferredoxin with iron chelating agents and 5,5′-dithio-bis-2-nitrobenzoic acid. Biochemistry 6, 3880–3891 (1967). Google Scholar
Matsubara, H.: Purification and some properties of _Scenedesmus_-Ferredoxin. J. biol. Chem. 243, 370–375 (1968). Google Scholar
—, Sasaki, R. M., Chain, R. K.: Spinach ferredoxin. II. Tryptic, chymotryptic, and thermolytic peptides, and complete amino acid sequence. J. biol. Chem. 243, 1732–1757 (1968). Google Scholar
Mayhew, S. G., Petering, D., Palmer, G., Foust, G. P.: Spectrophotometric titration of ferredoxins and Chromatium high potential iron protein with sodium dithionite. J. biol. Chem. 244, 2830–2834 (1969). Google Scholar
Orme-Johnson, W. A., Hansen, R. E., Beinert, H., Tsibris, J. C. M., Bartholomaus, R. C., Gunsalus, I. C.: On the sulfur components of iron-sulfur proteins. Proc. nat. Acad. Sci. (Wash.) 60, 368–372 (1968). Google Scholar
Palmer, G., Sands, R. H.: On the magnetic resonance of spinach ferredoxin. J. biol. Chem. 241, 253 (1966). Google Scholar
San Pietro, A.: Photochemical reduction of triphosphopyridine nucleotide by chloroplasts. In: Brookhaven Symposia in Biology, vol. 11, p. 262–270, Hrsg. R. C. Fuller u. a. Upton, N. Y.: Brookhaven Natl. Laboratory 1959. Google Scholar
Shin, M., Tagawa, K., Arnon, D. I.: Crystallization of ferredoxin-TPN reductase and its role in the photosynthetic apparatus of chloroplasts. Biochem. Z. 338, 84–96 (1963). Google Scholar
Sobel, B. E., Lovenberg, W.: Characteristics of Clostridium pasteurianum ferredoxin in oxidation-reduction reactions. Biochemistry 5, 6–13 (1966). Google Scholar
Tagawa, K., Arnon, D. I.: Oxidation-reduction potentials and stoichiometry of electron transfer in ferredoxins. Biochim. biophys. Acta (Amst.) 153, 602–613 (1968). Google Scholar
Tanaka, M. T., Nakashima, A., Benson, H., Mover, H., Yasunobu, K. T.: The amino acid sequence of Clostridium pasteurianum ferredoxin. Biochemistry 5, 1666–1681 (1966). Google Scholar
Tsibris, J. C. M., Tsai, R. L., Gunsalus, I. C., Orme-Johnson, W. H., Hansen, R. E., Beinert, H.: The number of iron atoms in the paramagenetic center (g=1.94) of reduced Putidaredoxin, a nonheme iron protein. Proc. nat. Acad. Sci. (Wash.) 59, 959–965 (1968). Google Scholar
Warburg, O., Christian, W.: Isolierung und Kristallisation des Gärungsferments Enolase. Biochem. Z. 310, 384–421 (1941/42). Google Scholar
Yamanaka, T.: Purification and some properties of ferredoxin derived from the blue-green alga Anacystis nidulans. Biochim. biophys. Acta (Amst.) 180, 196–198 (1969). Google Scholar