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Pure Appl. Chem., 1973, Vol. 34, No. 3-4, pp. 553-578

http://dx.doi.org/10.1351/pac197334030553

The plant ferredoxins and their relationship to the evolution of ferredoxins from primitive life

D. O. Hall, R. Cammack and K. K. Rao

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  • Antal Taras K., Kovalenko Ilya B., Rubin Andrew B., Tyystjärvi Esa: Photosynthesis-related quantities for education and modeling. Photosynth Res 2013, 117, 1. <http://dx.doi.org/10.1007/s11120-013-9945-8>
  • Siddhanta A.K., Bhattacharyya B.D.: ���Mexican-hat��� parameters of a non-heme protein. Journal of Molecular Structure: THEOCHEM 1989, 184, 39. <http://dx.doi.org/10.1016/0166-1280(89)85132-2>
  • Coutelle R., Hofacker G.L.: Influence of selective processes on the amino acid compositions of proteins: Collagen, cytochrome c, ferredoxin and α-crystallin. J Theor Biol 1982, 95, 615. <http://dx.doi.org/10.1016/0022-5193(82)90345-9>
  • Petersson Leif, Cammack Richard, Krishna Rao K., Siemankowski Raymond F., Richard Zobel C., Manuel H., Herskovits Theodore T., Elbaum Danek: Antiferromagnetic exchange interaction in the two-iron-two-sulphur ferredoxin from the blue-green alga Spirulina maxima studied with a highly sensitive magnetic balance. Biochimica et Biophysica Acta (BBA) - Protein Structure 1980, 622, 18. <http://dx.doi.org/10.1016/0005-2795(80)90154-3>
  • Nika Heinz, Hultin Tore, Bertrand Patrick, Gayda Jean-Pierre, Shimizu Toru, Nozawa Tsunenori, Hatano Masahiro, Satake Haruhiko, Imai Yoshio, Hashimoto Chikako, Sato Ryo: Disulfide interaction in situ between two neighbouring proteins in mammalian 60-S ribosomal subunits. Biochimica et Biophysica Acta (BBA) - Protein Structure 1979, 579, 10. <http://dx.doi.org/10.1016/0005-2795(79)90091-6>
  • Hase T., Wakabayashi S., Wada K., Matsubara H., Jüttner F., Rao K.K., Fry I., Hall D.O.: Cyanidium caldarium ferredoxin: a red ag̵al type?. FEBS Letters 1978, 96, 41. <http://dx.doi.org/10.1016/0014-5793(78)81058-8>
  • Hase Toshiharu, Wakabayashi Sadao, Matsubara Hiroshi, Rao K.Krishna, Hall David O., Widmer Herbert, Gysi Jurg, Zuber Herbert: The amino acid sequence of ferredoxin from the alga Mastigocladus laminosus. Phytochemisry 1978, 17, 1863. <http://dx.doi.org/10.1016/S0031-9422(00)88721-X>
  • de la Torre Angel, Chueca Ana, López Gorgé Julio: Isolation and properties of crystalline ferredoxin from lactuca sativa. Phytochemistry 1978, 17, 35. <http://dx.doi.org/10.1016/S0031-9422(00)89675-2>
  • Hazan G., Haas E., Steinberg I.Z., Gayda Jean-Pierre, Gibson John F., Cammack Richard, Hall David O., Mullinger Roger, Renugopalakrishnan V., Rein Robert: The fluorescence decay of human serum albumin and its subfractions. Biochimica et Biophysica Acta (BBA) - Protein Structure 1976, 434, 144. <http://dx.doi.org/10.1016/0005-2795(76)90045-3>
  • Kwanyuen P., Wildman S.G.: Nuclear DNA codes for Nicotiana ferredoxin. Biochimica et Biophysica Acta (BBA) - Protein Structure 1975, 405, 167. <http://dx.doi.org/10.1016/0005-2795(75)90327-X>
  • Wada Keishiro, Hase Toshiharu, Tokunaga Hiroko, Matsubara Hiroshi: Amino acid sequence of spirulina platensis ferredoxin: A far divergency of blue-green algal ferredoxins. FEBS Letters 1975, 55, 102. <http://dx.doi.org/10.1016/0014-5793(75)80969-0>
  • Andrew Peter W., Delaney Maria E., Rogers Lyndon J., Smith Arnold J.: Isolation and properties of a ferredoxin from Anabaena Flos-Aquae. Phytochemisry 1975, 14, 931. <http://dx.doi.org/10.1016/0031-9422(75)85161-2>
  • Scawen Michael D, Hewitt Eric J, James Douglas M: Preparation, crystallization and properties of Cucurbita pepo plastocyanin and ferredoxin. Phytochemisry 1975, 14, 1225. <http://dx.doi.org/10.1016/S0031-9422(00)98599-6>
  • Thomas B.R.: Sequence diagrams and the presentation of structural and evolutionary relationships among proteins. Biochemie 1975, 57, 271. <http://dx.doi.org/10.1016/S0300-9084(75)80302-6>