By Kenneth D. Karlin, Shinobu Itoh, Steven Rokita
Covers the drastically increasing topic of oxidative tactics mediated by means of copper ions inside organic systems
Copper-mediated organic oxidations supply a vast diversity of essentially vital and in all probability functional chemical tactics that pass many chemical and pharmaceutical disciplines. This most up-to-date quantity within the Wiley Series on Reactive Intermediates in Chemistry and Biology is split into 3 logical components in the subject of copper/oxygen chemistry— organic structures, idea, and bioinorganic types and applications—to discover the biosphere for its hugely developed and therefore effective oxidative modifications within the discovery of recent different types of interactions among molecular oxygen and copper ion. that includes a various selection of subject material unified in a single whole and finished source, Copper-Oxygen Chemistry probes the elemental facets of copper coordination chemistry, man made natural chemistry, and organic chemistry to bare either the organic and chemical facets using the present interesting study efforts at the back of copper-oxygen chemistry. additionally, Copper-Oxygen Chemistry:
Addresses the considerably expanding literature on oxygen-atom insertion and carbon-carbon bond-forming reactions in addition to enantioselective oxidation chemistries
Progresses from organic platforms to spectroscopy and thought, and onward to bioinorganic versions and applications
Covers a big selection of response kinds corresponding to insertion and dehydrogenation reactions that make the most of the inexpensive, considerable, and energy-containing O2 molecule
With thorough insurance through in demand authors and researchers shaping suggestions during this turning out to be box, this precious reference is key interpreting for bioinorganic chemists, in addition to natural, artificial, and pharmaceutical chemists in academia and undefined.
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Additional resources for Copper-Oxygen Chemistry (Wiley Series of Reactive Intermediates in Chemistry and Biology)
25. Prigge, S. ; Eipper, B. ; Mains, R. ; Amzel, L. M. Amidation of bioactive peptides: The structure of peptidylglycine a-hydroxylating monooxygenase Science 1997, 278, 1300–1305. 26. Boswell, J. ; Reedy, B. ; Blackburn, N. J. Structural investigations on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine a-amidating enzyme Biochemistry 1996, 35, 12241–12250. 27. Reedy, B. ; Blackburn, N. J. Preparation and characterization of half-apo dopamineb-hydroxylase by selective removal of CuA.
Fungal FDOs contain a mononuclear Cu2þ center, whereas the enzyme from Bacillus subtilis is presumed to prefer Mn2þ as cofactor,14–17 despite having been purified as an iron enzyme from a recombinant Escherichia coli clone. In contrast to the enzymes from B. , and Penicillium olsonii,11 the FDO protein of Streptomyces sp. 32,33 First, we give a brief overview of the studies on the enzymatic reaction and the structure of the enzymatic active site from A. japonicus. A more detailed insight will be presented into the mechanistic details of the oxygenation reactions including the mode of the O2 activation carried out with model substrates.
Timmers, H. J. L. ; Wevers, R. ; Lenders, J. W. M. Congenital dopamineb-hydroxylase deficiency in humans Ann. N. Y. Acad. Sci. 2004, 1018, 520–523. 8. Cubells, J. ; Zabetian, C. P. Human genetics of plasma dopamine b-hydroxylase activity: Applications to research in psychiatry and neurology Psychopharmacology 2004, 174, 463–476. 9. Prigge, S. ; Mains, R. ; Eipper, B. ; Amzel, L. M. New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function Cell Mol. Life Sci.