Biochemistry Online: An Approach Based on Chemical Logic

Biochemistry Online

CHAPTER 8 - OXIDATION/PHOSPHORYLATION 

B:  OXIDATIVE ENZYMES

BIOCHEMISTRY - DR. JAKUBOWSKI

 04/15/16

Learning Goals/Objectives for Chapter 8B:  After class and this reading, students will be able to

  • state the type of oxidizing reagent used and the products forms on oxidation reactions catalyzed by dehydrogenases, monoxygenases (hydroxylases), dioxygenases, and oxidases;
  • draw the reactive end of NAD+ and mechanisms showing it's reactions with substrates in enzyme-catalyzed two electron oxidation reactions;
  • explain differences in chemical reactivity of NAD+ and FAD in one and two electrons oxidations and with dioxygen;
  • describe the stereochemistry of the alcohol dehydrogenase-catalyzed oxidation of prochiral ethanol by NAD+;
  • explain why FAD/FADH2 are often tightly bound to dehydrogenases in contrast to NAD+/NADH where are freely diffusable substrates;
  • given standard reduction potentials, determine the ΔGo' for given redox reactions;
  • explain why different FAD and other flavin containing dehydrogenases have varying standard reduction potentials for the flavin but NAD+ dependent dehydrogenase have only one;
  • describe the role of heme in mono- and dioxygenases in activating dioxygen and minimizing side reactions of ROSs;
  • describe the biological role of cytochrome P450s;
  • define and give examples of oxidases;
  • compare the contrast the role of the heme in carrying hemoglobin and myoglobin, monoxygenases, and in oxidases.

B10.  Links and References

  1. Marshall, N. et al.  Rationally tuning the reduction potential of a single cupredoxin beyond the natural range Nature 462, 113 (2009)

  2. Zhao et al. Negative regulation of the deacetylase SIRT1 by DBC1.  Nature 451, 587-590 (2008)
  3. Marie Lagouge, M., ...., Auwerx, J. Resveratrol Improves Mitochondrial Function and Protects against Metabolic Disease by Activating SIRT1 and PGC-1α.  10.1016/j.cell.2006.11.013 (Nov 2006)
  4. Baur, J., ...., Sinclair, D.  Resveratrol improves health and survival of mice on a high-calorie diet.  Nature 444, 337 - 342 (2006)
  5. Myronova, N. et al.  Three-Dimensional Structure Determination of a Protein Supercomplex That Oxidizes Methane to Formaldehdye in Methylococcus capsulatus (Bath).  Biochemistry, 45, 11905 (2006)
  6. Wood et al. Sirutin activators mimic caloric restriction and delay ageing in metazoans.  Nature. 430, pg 686 (2004)
  7. Anderson, R. et al. Yeast life span extension by caloric restriction is independent of NAD fluctuation.  Science. 302, pg 2124 (2003)
  8. Hydrogenases:  Science, 299, pg 1686 (2003)
  9. Aguilaniu, H. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science, 299, pg 1751 (2003)
  10. Jump, D. The Biochemistry of n-3 polyunsaturated fatty acids. J. Biol. Chem. 277, pg 8755 (2002)
  11. Finney, L. and O'Halloran, T. Transition Metal Speciation in the Cell:  Insights from the Chemistry of Metal Ion Receptors. Science, 300, pg 931 (2003).
  12. Ohtake et al. Modulation of estrogen receptor signaling by association with the activated dioxin receptor. Nature 423, pg 487, 545 (2003) 
  13. Bazan, N. G. and Flower, R.J. Lipid Signals in Pain Control.  Nature. 420, pg 135 (2002)
  14. Kiefer et al. Structural Insights into the stereochemistry of the cyclooxgenase reaction. Nature. 405, pg 97 (2000)
  15. Marnett et al., Arachidonic Acid Oxygenation by COX-1 and COX-2.  J. Biol. Chem. 274, pg 22903 (1999)
  16. Oxygenase Pathways: Oxo, Peroxo, and Superoxo.  Science. 292, pg 651 (2001)
  17. Malkowski et al. The Productive Conformation of Arachidonic Acid Bound to Prostaglandin Synthase.  Science. 289. pg 1933 (2000)
  18. Lin et al. Requirement of NAD and SIR2 for Life-Span Extension by Calorie Restriction in S. Cerevisiae.  (role of NAD) Science. 289. pg 2062, 2126 (2000)
  19. Imai, S. et al.  Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase.  Nature, 403, 795 (2000)
  20. Landry, et. al. The silencing protein Sir2 and its homologs are NAD-dependent protein deacetylases.  PNAS, 97, pp 5807 (2000)
  21. A radical approach to (cancer) treatment (reactive O2 species).  Nature. 407, pg 309, 390 (2000)
  22. Melov et al. Extension of LIfe-Span with Superoxide Dismutase/Catalase Mimetics.  Science.  289. pg 1567 (2000)
  23. Anti-inflammatories inhibit cancer growth - but how?  (about cyclooxygenase I and II)  Science. 291. pg 581 (2001)
  24. Schlicthling et al. The catalytic pathway of cytochrome P450cam at atomic resolution.  Science. 287, pg 16 (2000)

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