#Question id: 10149

Formation of supramolecular complexes with regulatory proteins how effects on the catalytic activity of chloroplast enzymes in the dark as well as in the light?

a.) glyceraldehyde-3-phosphate dehydrogenase binds noncovalently with phosphoribulokinase and CP12 form a ternary complex, wherein glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase are catalytically inactive in the dark condition

b.) The A2B2 glyceraldehyde-3-phosphate dehydrogenase can form the A8B8 oligomer, Under dark conditions

c.) Reduced thioredoxin cleaves the disulfide bonds of CP12 and phosphoribulokinase, due to the reduction separates the components of the ternary complex releasing the active phosphoribulokinase and the active A4B4-glyceraldehyde 3-phosphate dehydrogenase under the light condition

d.) Reduced thioredoxin (Trx) cleaves the disulfide bond in subunit B of A8B8-glyceraldehyde-3-phosphate dehydrogenase, the reduction converts the active oligomer into the inactive A2B2-glyceraldehyde3-phosphate dehydrogenase under the light condition

Which of the following combination about catalytic activity in dark and the light is true?