Somayeh Farahmand; Faezeh Fatemi; Marzieh Dehghan Shasaltaneh; Reza Haji Hosseini; Shahriar Saeedyan
Abstract
In Acidithiobacillus ferrooxidans, proteins, like CoxB, present in the electron transmission pathway. The structure of CoxB has two copper atoms (CuA, CuB). CuA plays an important role in electron transport. According to previous studies, the conversion of histidine to methionine in a similar protein ...
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In Acidithiobacillus ferrooxidans, proteins, like CoxB, present in the electron transmission pathway. The structure of CoxB has two copper atoms (CuA, CuB). CuA plays an important role in electron transport. According to previous studies, the conversion of histidine to methionine in a similar protein leads to an increase the stability of protein and to improve its function. Also, the binding of methionine to CuB in the wild protein structure is another reason for the selection of the H230M mutation in CuA site. Wild-type and H230M mutants are simulated in the presence of a bilayer membrane POPC using the gromacs version 5.1.4. The conformational changes of mutated protein were investigated by RMSD, RMSF, SASA, Rg, DSSP, density, MSD, thickness, PCA, ED, DCCM and FEL analysis. The results of the wild protein and H230M mutant analysis show that the bacteria still preserves its sustainability after mutation. It seems that the H230M mutation leads to the increase of the amount of electron reception that requires further studies in this regard. Molecular dynamic simulation and principal component analysis provide compelling evidence that this H230M mutation contributes to increase the stability of protein. Thus, this finding defines new approaches in structural properties, accurate survey, and probability improves the electron transfer.
