Molecular characterization and expression analysis of copper‐zinc superoxide dismutases from the freshwater alga Closterium ehrenbergii under metal stress

2019 ◽  
Vol 35 (1) ◽  
pp. 5-14 ◽  
Author(s):  
Hui Wang ◽  
Jang‐Seu Ki
Keyword(s):  
Molecular Characterization ◽  
Expression Analysis ◽  
Metal Stress ◽  
Freshwater Alga ◽  
Superoxide Dismutases ◽  
Closterium Ehrenbergii ◽  
Copper Zinc ◽  
Copper Zinc Superoxide Dismutases

scholarly journals Direct Probing of Copper Active Site and Free Radical Formed during Bicarbonate-dependent Peroxidase Activity of Bovine and Human Copper,Zinc-superoxide Dismutases

2004 ◽  
Vol 279 (31) ◽  
pp. 32534-32540 ◽  
Author(s):  
Chandran Karunakaran ◽  
Hao Zhang ◽  
John P. Crow ◽  
William E. Antholine ◽  
B. Kalyanaraman
Keyword(s):  
Free Radical ◽  
Peroxidase Activity ◽  
Active Site ◽  
Superoxide Dismutases ◽  
Copper Zinc ◽  
Copper Zinc Superoxide Dismutases

scholarly journals The exchange of histidine C-2 protons in superoxide dismutases. A novel method for assigning histidine-metal ligands in proteins

1979 ◽  
Vol 183 (1) ◽  
pp. 127-132 ◽  
Author(s):  
A E G Cass ◽  
H A O Hill ◽  
J V Bannister ◽  
W H Bannister ◽  
V Hasemann ◽  
...  
Keyword(s):  
Metal Ion ◽  
Superoxide Dismutases ◽  
Metal Ion Binding ◽  
Histidine Residues ◽  
Copper Zinc Superoxide Dismutase ◽  
Metal Ligands ◽  
Zinc Superoxide Dismutase ◽  
Selective Deuteration ◽  
Copper Zinc ◽  
Copper Zinc Superoxide Dismutases

The rates of exchange of the C-2 protons of histidine residues in copper-zinc superoxide dismutase are substantially decreased by metal ion binding. This observation was used to distinguish between ligand and non ligand histidine residues in bovine and yeast copper-zinc superoxide dismutases; the effect was shown to depend only on metal ion co-ordination and not as a consequence of concomitant changes in protein structure. Selective deuteration of the zinc-only proteins at pH (uncorrected pH-meter reading) 8.2 and 50 degrees C resulted in the distinction between copper and zinc ligand resonances in the 1H n.m.r. spectrum of the enzymes. This method is proposed as a generally applicable technique for identifying histidine residues as ligands in metalloproteins.

scholarly journals Nonamyloid Aggregates Arising from Mature Copper/Zinc Superoxide Dismutases Resemble Those Observed in Amyotrophic Lateral Sclerosis

2010 ◽  
Vol 285 (53) ◽  
pp. 41701-41711 ◽  
Author(s):  
Young-Mi Hwang ◽  
Peter B. Stathopulos ◽  
Kristin Dimmick ◽  
Hong Yang ◽  
Hamid R. Badiei ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Superoxide Dismutases ◽  
Copper Zinc ◽  
Copper Zinc Superoxide Dismutases ◽  
Lateral Sclerosis

Manganese ad copper-zinc superoxide dismutases in the developing rat retina

1997 ◽  
Vol 99 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Tsukihiko Ogawa ◽  
Akihiro Ohira ◽  
Tsugio Amemiya
Keyword(s):  
Superoxide Dismutases ◽  
Rat Retina ◽  
Copper Zinc ◽  
Copper Zinc Superoxide Dismutases ◽  
Developing Rat

Metal-deficient copper-zinc superoxide dismutases

1982 ◽  
Vol 215 (1) ◽  
pp. 116-128 ◽  
Author(s):  
Sandra L. Jewett ◽  
Gregory S. Latrenta ◽  
Carol M. Beck
Keyword(s):  
Superoxide Dismutases ◽  
Copper Zinc ◽  
Copper Zinc Superoxide Dismutases

Differential regulation of manganese and copper/zinc superoxide dismutases by the facial nerve transection

1992 ◽  
Vol 582 (2) ◽  
pp. 342-345 ◽  
Author(s):  
T. Yoneda ◽  
S. Inagaki ◽  
Y. Hayashi ◽  
T. Nomura ◽  
H. Takagi
Keyword(s):  
Facial Nerve ◽  
Differential Regulation ◽  
Superoxide Dismutases ◽  
Nerve Transection ◽  
Copper Zinc ◽  
Copper Zinc Superoxide Dismutases
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