Carbon monoxide binding to the heme group at the dimeric interface modulates structure and copper accessibility in the Cu,Zn superoxide dismutase fromHaemophilus ducreyi: in silico andin vitroevidences

2012 ◽  
Vol 30 (3) ◽  
pp. 269-279 ◽  
Author(s):  
Giovanni Chillemi ◽  
Serena De Santis ◽  
Mattia Falconi ◽  
Giordano Mancini ◽  
Valentina Migliorati ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Superoxide Dismutase ◽  
In Silico ◽  
Heme Group ◽  
Dimeric Interface ◽  
Carbon Monoxide Binding

10-gingerol induces oxidative stress through HTR1A in cumulus cells: in-vitro and in-silico studies

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Kiptiyah Kiptiyah ◽  
Widodo Widodo ◽  
Gatot Ciptadi ◽  
Aulanni’am Aulanni’Am ◽  
Mohammad A. Widodo ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Culture ◽  
Superoxide Dismutase ◽  
In Silico ◽  
Cumulus Cell ◽  
Cumulus Cells ◽  
Sod Activity ◽  
In Silico Studies ◽  
Incubation Periods

AbstractBackgroundWe investigated whether 10-gingerol is able to induce oxidative stress in cumulus cells.MethodsFor the in-vitro research, we used a cumulus cell culture in M199, containing 10-gingerol in various concentrations (0, 12, 16, and 20 µM), and detected oxidative stress through superoxide dismutase (SOD) activity and malondialdehyde (MDA) concentrations, with incubation periods of 24, 48, 72, and 96 h. The obtained results were confirmed by in-silico studies.ResultsThe in-vitro data revealed that SOD activity and MDA concentration increased with increasing incubation periods: SOD activity at 0 µM (1.39 ± 0.24i), 12 µM (16.42 ± 0.35ab), 16 µM (17.28 ± 0.55ab), 20 µM (17.81 ± 0.12a), with a contribution of 71.1%. MDA concentration at 0 µM (17.82 ± 1.39 l), 12 µM (72.99 ± 0.31c), 16 µM (79.77 ± 4.19b), 20 µM (85.07 ± 2.57a), with a contribution of 73.1%. Based on this, the in-silico data uncovered that 10˗gingerol induces oxidative stress in cumulus cells by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.Conclusions10-gingerol induces oxidative stress in cumulus cells through enhancing SOD activity and MDA concentration by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.

scholarly journals Amino Acid Substitution at the Dimeric Interface of Human Manganese Superoxide Dismutase

2003 ◽  
Vol 279 (7) ◽  
pp. 5861-5866 ◽  
Author(s):  
Amy S. Hearn ◽  
Li Fan ◽  
James R. Lepock ◽  
James P. Luba ◽  
William B. Greenleaf ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Amino Acid ◽  
Amino Acid Substitution ◽  
Manganese Superoxide Dismutase ◽  
Dimeric Interface ◽  
Manganese Superoxide

scholarly journals Oxidation of glycine by Phaseolus leghaemoglobin with associated catabolic reactions at the haem

1978 ◽  
Vol 176 (2) ◽  
pp. 351-358 ◽  
Author(s):  
P Lehtovaara
Keyword(s):  
Hydrogen Peroxide ◽  
Carbon Monoxide ◽  
Superoxide Dismutase ◽  
Phaseolus Vulgaris ◽  
Initial Velocity ◽  
Root Nodules ◽  
Green Product ◽  
Oxygen Complex ◽  
Optimum Ph ◽  
Glycine Oxidase

Leghaemoglobin from the root nodules of kidney bean (Phaseolus vulgaris) reacts in alkaline glycine solutions as a glycine oxidase in a reaction that may also be regarded as a coupled oxidation. Leghaemoglobin is reduced to the ferrous form by glycinate, the oxygen complex is formed, and finally the haem is attacked to yield a green reaction product. Glycine is simultaneously oxidized to glyoxylate, and hydrogen peroxide is generated. The initial velocity of the formation of the green product is proportional to the concentrations of leghaemoglobin and glycine, and the optimum pH for the reaction is 10.2. The green product is not formed if carbon monoxide, azide of imidazole is bound to the haem, whereas oxidation of glycine to glyoxylate is not inhibited by azide and not essentially by carbon monoxide. Haem breakdown is activated by digestion of leghaemoglobin by carboxypeptidase, and partly inhibited by catalase and superoxide dismutase.

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