Answer:
(B) They may have binding sites for regulatory molecules that are separate from active sites.
(C) They generally have more than one subunit.
(E) They interconvert between a more active form and a less active form.
Explanation:
Allosteric enzymes are the regulatory enzymes that have a specific site for binding of modulator or effector molecule. The activity of these enzymes is altered by the noncovalent binding of modulators at the allosteric site. The binding of the modulator brings about a conformational change in the allosteric enzymes.
The relatively inactive conformation of these enzymes is called T state while the active conformation is the R state. Most of the allosteric enzymes have multiple subunits and deviate from Michaelis–Menten kinetics and exhibit a sigmoid saturation curve of V0 vs. [S].
<span>3.2 inches. The nurse if doing a cardiopulmonary resuscitation. It is an emergency procedure combines with chest compression and artificial ventilation. It is done during a cardiac arrest. When doing so the nurse should compress the lower sternum by 3.2 inches.</span>
Answer:
transport of protons (H+) from low concentration in the mitochondrial matrix to high concentration in the mitochondrial intermembrane space
Explanation:
atpase pump can also be called atp synthase. this enzyme catalyses atp formation from adenosine diphosphate and phosphate. it has f1, stalk and f0 components. 3 positive hydrogen ions go through to make 1 adenosine triphosphate molecule. oxidative phosphorylation has to do with the loss of electrons. there would be electrons loss from NADH to FADH2. Cytochromes carries them through different series of transferases from I to IV and while on this positive hydrogen ions are released into mitochondrial matrix
positive hydrogen ions are moved back to lumen through adenosine triphosphate channels. a process called chemiosmosis. the pro
Answer:srry, i dont know the answer
