Rolf Brändén
Affiliations: | Department of Biochemistry and Biophysics | University of Gothenburg, Gothenburg, Västra Götalands län, Sweden |
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Publications
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Janson K, Brändén R. (1991) A spectrometric study of the Co2+-activated ribulose-1,5-bisphosphate carboxylase reaction during turnover and at different pH Biochimica Et Biophysica Acta. 1080: 40-44 |
Brändén R, Janson K, Nilsson P. (1989) Studies of the Co2+-activated ribulose-1,5-bisphosphate carboxylase/oxygenase by the use of spectrophotometry. Biochimica Et Biophysica Acta. 995: 75-81 |
Brändén R, Janson K, Nilsson P, et al. (1987) Intermediates formed by the Co2+-activated ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach studied by electron paramagnetic resonance spectroscopy. Biochimica Et Biophysica Acta. 916: 298-303 |
Styring S, Brändén R. (1985) Co2+- and Cu2+-incubated ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum studied with electron paramagnetic resonance spectroscopy Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 832: 113-118 |
Nilsson T, Brändén R, Styring S. (1984) Distortion of the activator metal coordination during the turnover of cobalt-activated ribulosebisphosphate carboxylase/oxygenase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 788: 274-280 |
Brändén R, Nilsson T, Styring S, et al. (1980) L-3-Phosphoglyceric acid, formed by ribulose-1,5-bisphosphate carboxylase, is the primary substrate for photorespiration. Experimental test of a hypothesis Biochemical and Biophysical Research Communications. 92: 1306-1312 |
Brändén R, Nilsson T, Styring S. (1980) The formation of L-3-phosphoglyceric acid by ribulose-1,5-bisphosphate carboxylase Biochemical and Biophysical Research Communications. 92: 1297-1305 |
Brändén R, Deinum J. (1978) The effect of pH on the oxygen intermediate and the dioxygen reducing site in blue oxidases Biochimica Et Biophysica Acta. 524: 297-304 |
Rosén S, Brändén R, Vänngård T, et al. (1977) EPR evidence for an active form of cytochrome c oxidase different from the resting enzyme. Febs Letters. 74: 25-30 |
Brändén R, Deinum J. (1977) Type 2 copper (II) as a component of the dioxygen reducing site in laccase: evidence from EPR experiments with 17O. Febs Letters. 73: 144-146 |