2009-10-16_-_Lecture_18

2009-10-16_-_Lecture_18 - Biochemistry 461 FS 2009 Michigan...

Info iconThis preview shows pages 1–4. Sign up to view the full content.

View Full Document Right Arrow Icon
Biochemistry 461 FS 2009 Michigan State University Bioenergetics: Phosphoryl Transfer October 16, 2009 Lecture 18 • The hydrolysis of ATP to ADP + P i has Δ G '° of -30.5 kJ/mol. • Why is it so large and negative? Hydrolysis of ATP is Exergonic ATP (Adenosine triphosphate) 2
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Hydrolysis of ATP is Exergonic • But Δ G '° is under standard conditions. In the cell we don’t have standard conditions. • We can calculate the change in free energy under intracellular conditions ( Δ G p ): 3 Hydrolysis of Phosphoenolpyruvate (PEP) • PEP also has a “high-energy phosphate bond.” • What do we really mean by high-energy phosphate bond? • In this case Δ G '° is even more negative than the hydrolysis of ATP. • What is responsible for the large, negative Δ G '° in this case? 4
Background image of page 2
Hydrolysis of Other Phosphate Compounds Phosphocreatine 1,3-Bisphosphoglycerate 5 • ATP is the “energy currency” of nearly all living organisms.
Background image of page 3

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Image of page 4
This is the end of the preview. Sign up to access the rest of the document.

Page1 / 6

2009-10-16_-_Lecture_18 - Biochemistry 461 FS 2009 Michigan...

This preview shows document pages 1 - 4. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online