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BioWiki: The Dynamic Biology Hypertext > Biochemistry > Oxidation and Phosphorylation > ATP and Oxidative Phosphorylation

ATP and Oxidative Phosphorylation

Table of Contents

Biological oxidation reactions serve two functions:

  1. Oxidation of organic molecules can produce new molecules with different properties (e.g., an increase in solubility is observed on hydroxylation of aromatic substrates by cytochrome P450) and Likewise, amino acids can be oxidized to produce neurotransmitters.
  2. Most biological oxidation reactions occur, however, to produce energy to drive thermodynamically unfavored biological processes such as protein and nucleic acid synthesis, or motility.

Chemical potential energy is not just released in biological oxidation reactions. Rather, it is transduced into a more useful form of chemical energy in the molecule ATP (adenosine triphosphate). This chapter will discuss the properties that make ATP so useful biologically, and how exergonic biological oxidation reactions are coupled to the synthesis of ATP.

  1. Properties of ATP
  2. Coupling of Oxidations/Synthesis of ATP Under Anaerobic Conditions
  3. Coupling of Ox/Phos Under Aerobic Conditions
  4. Recent Confirmation of the Boyer Hypothesis
  5. How Does the pH Gradient Collapse Lead to ATP Synthesis?
  6. Can a Proton Gradient Supply Enough Energy for ATP Synthesis?


  1. Wantanbe, R. et al. Nature Chemical Biology, 6, 814-820 (2010)
  2. Vander Heiden, M. et al. Understanding the Warburg Effect: The metabolic requirements of cell proliferation.  Science 234, pg 1029 (2009).
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  6. Rastogi and Girvin. Structural changes linked to proton translocation by subunit c of the ATP synthase.  Nature. 402, pg 263 (1999)
  7. Larsen et al.  Dietary Advice on Q and Extension of Life-Span in C. Elegans by a Diet Lacking Coenzyme Q (free radicals and aging?). Science. 295, pg 54, 120 (2002)
  8. Lower et al. How Bacteria Respire minerals.  Science. 292. pg 1312, 1360 (2001)
  9. Echtay et. al. Coenzyme Q is an obligatory cofactor for uncoupling protein function.  Nature 408, pg 609 (2000)
  10. Chen et al. Atomically defined mechanism for proton transfer to a buried redox center in a protein. Nature. 405, pg 814 (2000)
  11. Echtay et al. Superoxide activates mitochondrial uncoupling proteins. Nature. 415. pg 96 (2002)
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00:36, 21 Nov 2013


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This material is based upon work supported by the National Science Foundation under Grant Numbers 1525057, and 1413739.

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