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Effect of Cationic and Anionic Porphyrins on the Structure and Activity of Adenosine Deaminase

  • Received : 2011.06.14
  • Accepted : 2011.07.29
  • Published : 2011.09.20

Abstract

Kinetic and structural studies have been carried out on the effects of meso-tetrakis(4-sulfonatophenyl)-porphyrin ($H_2TPPS_4$) as an anionic and meso-tetrakis(3-N-methyl-pyridyl)porphyrin ($H_2TMPYP$) as a cationic porphyrin with adenosine deaminase (ADA) in 25 mM citrate/phosphate buffer, pH = 4-8, at $37^{\circ}C$ using UVvis spectrophotometry, circular dichroism (CD), fluorescence spectrophotometry as well as molecular dynamics (MD) and molecular docking. Kinetic results showed that the two porphyrins are non-competitive inhibitors. Increasing pH, increases $K_I$ and cationic porphyrin has a higher $K_I$ and lower binding constant ($K_b$) at all pH ranges. Analyzing the secondary structure revealed that both ligands decrease the secondary structure and that the anionic porphyrin is more effective.

Keywords

References

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