TY - JOUR
T1 - Ferredoxin-NADP+ oxidoreductase is the respiratory NADPH dehydrogenase of the cyanobacterium Anabaena variabilis
AU - Scherer, Siegfried
AU - Alpes, Irene
AU - Sadowski, Heike
AU - Böger, Peter
N1 - Funding Information:
This work was supported by the Deutsche For-sehungsgemeinschaft. The technical assistance of Regina Grimm and Marlies Klett is gratefully acknowledged. The authors are grateful to Dr. A. Serrano comments on the manuscript.
PY - 1988/11/15
Y1 - 1988/11/15
N2 - The NADPH dehydrogenase of the cyanobacterium Anabaena variabilis was solubilized, purified, and characterized. Activity staining after nondenaturing polyacrylamide gel electrophoresis, kinetics, and immunological characterization led to the conclusion that only one thylakoid-associated NADPH dehydrogenase exists in Anabaena, identical with ferredoxin-NADP+ oxidoreductase (FNR). After sodium dodecyl sulfatepolyacrylamide gel electrophoresis an intense band at 34 kDa and a weak band at 52 kDa were found by immunoblotting with an antibody against Anabaena FNR. Using a cellfree preparation competent of oxidative phosphorylation it was demonstrated that FNR operates as a respiratory NADPH dehydrogenase coupled to cyanide-sensitive oxidative ATP formation.
AB - The NADPH dehydrogenase of the cyanobacterium Anabaena variabilis was solubilized, purified, and characterized. Activity staining after nondenaturing polyacrylamide gel electrophoresis, kinetics, and immunological characterization led to the conclusion that only one thylakoid-associated NADPH dehydrogenase exists in Anabaena, identical with ferredoxin-NADP+ oxidoreductase (FNR). After sodium dodecyl sulfatepolyacrylamide gel electrophoresis an intense band at 34 kDa and a weak band at 52 kDa were found by immunoblotting with an antibody against Anabaena FNR. Using a cellfree preparation competent of oxidative phosphorylation it was demonstrated that FNR operates as a respiratory NADPH dehydrogenase coupled to cyanide-sensitive oxidative ATP formation.
UR - http://www.scopus.com/inward/record.url?scp=0024289227&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(88)90027-6
DO - 10.1016/0003-9861(88)90027-6
M3 - Article
C2 - 2461678
AN - SCOPUS:0024289227
SN - 0003-9861
VL - 267
SP - 228
EP - 235
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -