An enzyme catalyzes the conversion of substrate S to product…

An enzyme catalyzes the conversion of substrate S to product P following classic Michaelis–Menten kinetics, with a Km of 4 mM and a Vmax of 200 μmol/min. When 8 mM of the inhibitor is added, the apparent Km increases to 12 mM while Vmax remains the same. Which of the following statements is most accurate regarding the inhibitor’s properties and the kinetic consequences of its binding?  

Hemoglobin’s ability to load oxygen in the lungs and unload…

Hemoglobin’s ability to load oxygen in the lungs and unload it in metabolically active tissues is governed by two key phenomena: the Bohr effect and positive cooperativity. Which of the following options best describes how these two mechanisms interact to optimize oxygen transport?