Step 1: Use the Michaelis-Menten equation.
The Michaelis-Menten equation for enzyme kinetics is:
\[
v = \frac{V_{\text{max}} [S]}{K_m + [S]},
\]
where \( v \) is the reaction velocity, \( V_{\text{max}} \) is the maximum velocity, \( [S] \) is the substrate concentration, and \( K_m \) is the Michaelis constant.
Step 2: Solve for \( K_m \).
At a substrate concentration of 5 mM, the reaction velocity is 0.2 mole/sec. We can substitute these values into the equation:
\[
0.2 = \frac{0.4 \times 5}{K_m + 5}.
\]
Solving for \( K_m \):
\[
0.2(K_m + 5) = 2 $\Rightarrow$ 0.2K_m + 1 = 2 $\Rightarrow$ 0.2K_m = 1 $\Rightarrow$ K_m = 5.
\]
Step 3: Use the value of \( K_m \) to calculate the rate at 10 mM substrate concentration.
Now, substitute \( K_m = 5 \) and \( [S] = 10 \) mM into the Michaelis-Menten equation:
\[
v = \frac{0.4 \times 10}{5 + 10} = \frac{4}{15} = 0.2667 \, \text{mole/sec}.
\]
Step 4: Conclusion.
The reaction rate at 10 mM substrate concentration is 0.267 mole/sec.
Which one of the following matches is CORRECT between the inhibitors given in Group A with their modes of action in Group B?
\[\begin{array}{|c|c|} \hline Group A & Group B \\ \hline \text{(P) Antimycin A} & \text{(i) Inhibits cytochrome c oxidase} \\ \hline \text{(Q) Amytal} & \text{(ii) Blocks electron transfer from cyt b to cyt c1} \\ \hline \text{(R) Carbon monoxide} & \text{(iii) Inhibits adenine nucleotide translocase} \\ \hline \text{(S) Atractyloside} & \text{(iv) Prevents electron transfer from Fe-S centers of complex 1 to ubiquinone} \\ \hline \end{array}\]