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Download Active Oxygen in Biochemistry by Raymond Y. N. Ho, Joel F. Liebman (auth.), Joan Selverstone PDF

By Raymond Y. N. Ho, Joel F. Liebman (auth.), Joan Selverstone Valentine, Christopher S. Foote, Arthur Greenberg, Joel F. Liebman (eds.)

ISBN-10: 0751402931

ISBN-13: 9780751402933

ISBN-10: 9401106096

ISBN-13: 9789401106092

The box of "Oxygen Activation" has attracted significant curiosity lately, not just since it offers demanding situations in these fields of simple examine that objective to appreciate the elemental elements of chemical and organic reactions that contain dioxygen, but additionally as a result of its wide variety of functional implications in such different fields as medication, synthesis of prescription drugs and different natural compounds, fabrics technology, and atmospheric technology. this can be the second one of 2 volumes that target the topic of oxygen activation, the 1st slanted towards chemistry and the second one towards organic chemistry. We deliberate those volumes to be extra common than many monographs of this kind, no longer as distinctive summaries of the authors' personal examine yet relatively as common overviews of the sphere. Our collection of themes was once strongly prompted by way of our syllabus for a direction entitled "Oxygen Chemistry," which people have two times taught together at UCLA. Definition of vital concerns, horizons, and destiny customers was once a tremendous objective, and, even if completely accomplished assurance used to be impossible, we think that we have got selected a consultant number of study themes present to the sphere. we have now specified this paintings to a various viewers starting from pros in fields from physics to drugs to starting graduate scholars who're drawn to speedily buying the fundamentals of this field.

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Extra resources for Active Oxygen in Biochemistry

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FEIG, A. , and LIPPARD, S. J. (1994) Reactions of Non-Heme Iron(II) Centers with Dioxygen in Biology and Chemistry. Chern. , 94, 759805. FREEDMAN, T. , LOEHR, J. , and LOEHR, T. M. (1976) A Resonance Raman Study of the Copper Protein Hemocyanin: New Evidence for the Structure of the Oxygen-Binding Site. J. Am. Chern. , 98, 28092815. GEORGE, P. (1965) The Fitness of Oxygen, in Oxidases and Related Redox Systems (T. E. King, H. S. Mason, and M. ), John Wiley and Sons, New York, pp. 3-36. References 33 GRIFFITH, J.

These effects are illustrated quantitatively by the rate constants of the reactions. We will also examine the fates of the enzyme-bound reactive oxygen species and again will compare these with model reactions when available. Flavins are versatile catalysts and are involved in a wide variety of redox reactions central to metabolism. Their ability to take part in either one- or two-electron transformations is one of their most important properties. Thus, flavin-utilizing enzymes are found in electron transport chains, where electrons from two-electron donors such as NADH are donated to one-electron acceptors such as cytochromes.

0 is -210mV, indicating that its oxidation to oxidized flavin by O2 is quite favorable. Protein-binding interactions can significantly increase or decrease this value. It is thought that when bound to enzymes, most reduced flavins exist as the anion (FIH-) rather than as the neutral molecule (FIH 2 ) (Muller, 1991b). The one-electron reduced flavin, the flavin semiquinone, can also exist as an anion or as a neutral molecule. The stability of the semiquinone depends on the relative reduction potential for each one-electron step.

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Active Oxygen in Biochemistry by Raymond Y. N. Ho, Joel F. Liebman (auth.), Joan Selverstone Valentine, Christopher S. Foote, Arthur Greenberg, Joel F. Liebman (eds.)


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