Oxidative stress is the imbalance of oxidants and reductants; it affects different parts of the organisms. In methane-producing archaea, Methanosarcina acetivorans, a rubrerythrin-like protein methanogen rubrerythrin, is involved in the oxidative defense of the microorganism. It is a 45 kDa homodimer protein in the buffer solution. ICPMS and EXAFS analyses confirmed the presence of iron and zinc in this protein's structure. EPR confirmed the iron (Fe3+) of the rubredoxin center with the characteristic peak in the low field having a 9.35 g value and a diiron center peak in the high field region with a characteristic 2.01 g value.
A BioSAXS analysis was conducted to investigate the structural changes in a mRbr under different conditions. The results revealed that the protein undergoes substantial structural modifications when exposed to either oxidation or reduction. When treated with H2O2, the protein sample displayed an Rg of 47Ao and a Dmax of 167 Ao, indicating a larger size than the reduced state. Conversely, when subjected to Na2S2O4, the protein sample had an Rg of 45 Ao and a Dmax of 45 Ao.
| Identifer | oai:union.ndltd.org:siu.edu/oai:opensiuc.lib.siu.edu:theses-4311 |
| Date | 01 August 2024 |
| Creators | Iftikhar, Muhammad |
| Publisher | OpenSIUC |
| Source Sets | Southern Illinois University Carbondale |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Theses |
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