Towards <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msup><mml:mtext>Al</mml:mtext><mml:mrow><mml:mn mathvariant="bold">3</mml:mn><mml:mo mathvariant="bold">+</mml:mo></mml:mrow></mml:msup></mml:math>-Induced Manganese-Containing Superoxide Dismutase Inactivation and Conformational Changes: An Integrating Study with Docking Simulations

<table>Inactivation kinetics of Mn-SOD in the presence of Al<sup>3+</sup>. (a) The Al<sup>3+</sup> concentrations were 0.2 (●), 0.3 (▲), and 0.4 mM (■), respectively. The reaction occurred at 25°C. The final concentration of Mn-SOD was 1.25 <i>μ</i>M. (b) The semilogarithmic plot. The Al<sup>3+</sup> concentration was 0.2 mM. (●) Experimental points. (+) Points obtained by subtracting the contribution of the slow phase from the data in the curve (- - -).</table>

Enzyme Research

fig2

Figure 2

Figure 2: Towards <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msup><mml:mtext>Al</mml:mtext><mml:mrow><mml:mn mathvariant="bold">3</mml:mn><mml:mo mathvariant="bold">+</mml:mo></mml:mrow></mml:msup></mml:math>-Induced Manganese-Containing Superoxide Dismutase Inactivation and Conformational Changes: An Integrating Study with Docking Simulations 

Figure 2 | Towards Al3+-Induced Manganese-Containing Superoxide Dismutase Inactivation and Conformational Changes: An Integrating Study with Docking Simulations 