The key reaction that led to Boyer’s proposed loose-tight-op…

The key reaction that led to Boyer’s proposed loose-tight-open mechanism for the reaction catalyzed by ATP synthase is shown below. The experiment was done in the presence of 18O labeled water with the free purified enzyme. It was the results of this experiment that led him to propose this unique mechanism of action for the synthesis of ATP by ATP synthase in the late 1950s. Briefly explain what aspect of this experiment implied that the ATP is formed by ATP synthase all by itself outside of the cell. (2 pts.) ADP + Pi + H2O18    

Questions 16-20 Identify the cofactor or parallel reaction f…

Questions 16-20 Identify the cofactor or parallel reaction for each question. Some answer options may be used more than once, and some answer options will not be used. Some questions have more than one acceptable answer that will receive credit.  Use the image below for questions 16-20. Answer Options for 16-19 Aldolase Aconitase Alpha ketoglutarate dehydrogenase complex Enolase Fumarase Hexokinase Pyruvate dehydrogenase complex Pyruvate kinase Succinyl CoA synthetase Succinate dehydrogenase     Image Description A stepwise biochemical pathway showing the conversion of a substrate into Acetyl CoA through six steps. The pathway begins with leucine. In step 1, leucine is deaminated, with the amine being replaced by a ketone. In step 2, the carboxylic acid is removed and replaced by SCoA. In step 3, a single bond between a CH and a CH2 is replaced by a double bond, both carbons losing one hydrogen in the process. In step 4, one of the methylene groups on the terminal end of the leucine’s R chain has a carboxylic acid attached to it. In step 5, the carbon-carbon double bond created in step 3 is removed, with the CH being converted back into CH2 and the C getting an alcohol attached to it. In step 6, acetyl CoA is removed from the structure.