What is the standard Gibbs free energy change (∆G°') when ATP is hydrolyzed to ADP and inorganic phosphate (Pi)?

Prepare for the UofT BCH210H1 Biochemistry I midterm with exam-like questions. Access detailed solutions and explanations for proteins, lipids, and metabolism topics. Strengthen your understanding and excel on test day!

The standard Gibbs free energy change (∆G°') for the hydrolysis of ATP to ADP and inorganic phosphate (Pi) is approximately -30.5 kJ/mol, which can be rounded to -31 kJ/mol. This negative value indicates that the reaction is exergonic, meaning it releases energy. This release of energy from ATP hydrolysis is a key driving force that powers many cellular processes, including muscle contraction, biosynthesis, and active transport.

In this context, the reaction describes the conversion of ATP (adenosine triphosphate) to ADP (adenosine diphosphate) and Pi, which is energetically favorable. The energy released during this reaction is significant enough that it is utilized by various enzymes and metabolic pathways to perform work within the cell. Thus, the standard Gibbs free energy change quantifies this energetic aspect, confirming why -31 kJ/mol is the correct representation for this hydrolysis reaction.

Subscribe

Get the latest from Examzify

You can unsubscribe at any time. Read our privacy policy