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

The box of "Oxygen Activation" has attracted massive curiosity lately, not just since it offers demanding situations in these fields of simple examine that objective to appreciate the basic features of chemical and organic reactions that contain dioxygen, but additionally as a result of its wide variety of functional implications in such assorted fields as drugs, synthesis of prescribed drugs and different natural compounds, fabrics technological know-how, 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 basic than many monographs of this type, no longer as distinct summaries of the authors' personal learn yet quite as basic overviews of the sector. Our number of themes used to be strongly encouraged via our syllabus for a direction entitled "Oxygen Chemistry," which folks have two times taught together at UCLA. Definition of significant concerns, horizons, and destiny customers was once a tremendous aim, and, even supposing absolutely finished assurance used to be impossible, we think that we have got selected a consultant choice of learn issues present to the sphere. now we have unique this paintings to a various viewers starting from pros in fields from physics to drugs to starting graduate scholars who're drawn to swiftly buying the fundamentals of this field.

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E. (1994) Vanadium Peroxide Complexes. Chern. , 94, 625-638. , and HALL, M. B. (1994) Theoretical Calculations of MetalDioxygen Complexes. Chern. , 94, 639-658. COLE, P. , and ROBINSON, C. H. (1991) Mechanistic Studies on a Placental Aromatase Model Reaction. J. Am. Chern. , 113, 8130-8137. COLLMAN, J. P. (1977) Synthetic Models for the Oxygen-Binding Hemoproteins. Acc. Chern. , 10, 265-272. COLLMAN, J. , BRAUMAN, J. , HALBERT, T. , and SUSLICK, K. S. (1976) Nature of O 2 and CO Binding to Metalloporphyrins and Heme Proteins.

ROBERTS, H. , and SYMES, W. R. (1968) The Reaction of Dipotassium Hydridotetracyanoaquorhodate(III) with Oxygen Dipotassium Hydroperoxotetracyanoaquorhodate(III). J. Chern. , 1450-1453. SAWAKI, Y. (1992) Peroxy Acids and Peroxy Esters, in Organic Peroxides (W. ), John Wiley & Sons, New York, pp. 425-477. SAWYER, D. T. , and HOOH) in Biology, in Oxygen Complexes and Oxygen Activation by Transition Metals (A. E. Martell and D. T. ), Plenum, New York, pp. 131-148. SAWYER, D. T. (1991) Oxygen Chemistry, Oxford University Press, New York.

Myoglobin, hemerythrin, or hemocyanin. In those cases, the metalloenzyme contains a substrate-binding site in close proximity to its dioxygen-binding site, and the bound dioxygen ligand is activated by reduction for reaction with the substrate. The oxygenase enzymes catalyze the reaction of dioxygen with organic or inorganic substrates. Such enzymes lower the kinetic barriers to such reactions by binding and activating either dioxygen or the substrate. There are two types of oxygenase enzymes: monooxygenase enzymes, which incorporate one of the oxygen atoms in O2 into the oxygenated products and reduce the other to water, and dioxygenase enzymes, which incorporate both oxygens into the oxygenated products.

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