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Advances in Inorganic Chemistry: Homogeneous Biomimetic Oxidation Catalysis - Rudi van Eldik, Jan Reedijk - Google Books
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href=\"https://books.google.com.sg/url?id=UgNp8-wq-aAC\u0026pg=PA95\u0026q=https://www.elsevier.com/books-and-journals\u0026clientid=ca-print-elsevier-academic_press\u0026linkid=1\u0026usg=AOvVaw1hufpoNvVr3WhSU8JGve-N\u0026source=gbs_pub_info_r\"\u003eElsevier\u003c/a\u003e","is_ebook":true,"volumeresult":{"has_flowing_text":false,"has_scanned_text":true,"can_download_pdf":false,"can_download_epub":false,"is_pdf_drm_enabled":false,"is_epub_drm_enabled":false},"publisher":"Elsevier","publication_date":"2006.01.18","subject":"Science","num_pages":298,"sample_url":"https://play.google.com/books/reader?id=UgNp8-wq-aAC\u0026source=gbs_vpt_hover","synposis":"Advances in Inorganic Chemistry Volume 58 focuses on homogeneous biomimetic oxidation catalysis. Contributions by leading experts in the field cover important advances in inorganic and bioinorganic chemistry. Contributions include diversity-based approaches to selective biomimetic oxidation catalysis; the selective conversion of hydrocarbons with H2O2 using biomimetic non-heme iron and manganese oxidation catalysis; DNA oxidation by copper and manganese complexes; influences of the ligand in copper-dioxygen complex-formation and substrate oxidations; biomimetic oxidations by dinuclear and trinuclear copper complexes. In the final contribution the authors focus on green oxidation of alcohols using biomimetic copper complexes and enzymes as catalysts. 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Control experiments established that it is indeed the intact peptide ligand that renders the Cu - ion catalytically active . For example , simple mixtures of\u0026nbsp;...","page_url":"https://books.google.com.sg/books?id=UgNp8-wq-aAC\u0026pg=PA17\u0026vq=redox\u0026dq=subject:%22Science+Chemistry%22"},{"page_id":"PA29","page_number":"29","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e enzymes D. Ligand design for biomimetic non - heme iron and manganese complexes III . Biomimetic iron catalysts A. Alkane hydroxylation B. cis - Dihydroxylation vs. olefin epoxidation C. Aromatic hydroxylation D. Role of additives\u0026nbsp;..."},{"page_id":"PA31","page_number":"31","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e enzymes . The focus of this review is on complexes that are able to catalyze hydrocarbon oxidation reactions using dihydrogen peroxide as oxidant . A. INTRODUCTION II . Biological Enzymes and Catalytic Oxidation In nature\u0026nbsp;..."},{"page_id":"PA32","page_number":"32","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e dismutation ( 176 ) Isopenicillin N synthase Isopenicillin N formation ( 177 ) Lipoxygenases Unsaturated fatty acid oxidation ( 178 ) Nitrile hydratase Nitrile to amide hydration ( 179 ) Rieske oxygenase Bleomycin Methane\u0026nbsp;..."},{"page_id":"PA34","page_number":"34","snippet_text":"... \u003cb\u003eREDOX\u003c/b\u003e ENZYMES Several enzymes are known, that naturally contain manganese in the active site and include classes as oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases, lectins, and integrins (24). Some representative\u0026nbsp;..."},{"page_id":"PA35","page_number":"35","snippet_text":"... \u003cb\u003eREDOX\u003c/b\u003e ENZYMES INVOLVED IN OXIDATIVE CONVERSIONS Enzyme class Superoxide dismutase Mn catechol dioxygenase Mn catalase Oxygen evolving complex Mn lipoxygenase Function Ref . Superoxide decomposition ( 190 ) Catechol oxidation ( 191 )\u0026nbsp;..."},{"page_id":"PA40","page_number":"40","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e cycle easily ( 46 ) . In fact , if not carried out in suitable organic solvents , the simple Fenton reaction will take place , involving Fell and dihydrogen peroxide , which is not very effective to carry out the oxidation of\u0026nbsp;..."},{"page_id":"PA60","page_number":"60","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e. couples. (. 135. ) . The. oxidation. potentials. of. the complexes generally increase with a more electron - donating nature of the substituents ( 135 ) . The use of Mn - phox complexes with the more electron - donating ligands\u0026nbsp;..."},{"page_id":"PA70","page_number":"70","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e enzymes . In : “ Metal Ions in Biological Systems ” ; vol . 37 , Marcel Dekker : New York , 2000 , p . 429 . 35. Yocum , C. F .; Pecoraro , V. L. Curr . Opin . Chem . Biol . 1999 , 3 , 182 . 36. Iwata , S .; Barber , J. Curr\u0026nbsp;..."},{"page_id":"PA77","page_number":"77","snippet_text":"... \u003cb\u003eRedox\u003c/b\u003e-active metal complexes have been known for decades to be able to mediate oxidative degradation of DNA. Because of the large literature on iron complexes, the most famous representatives of which are Fe-bleomycin and Fe-edta, this\u0026nbsp;..."},{"page_id":"PA79","page_number":"79","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e events has been proposed for the generation of the active species (Fig. 3). The CuII complex is ¢rst reduced to the CuI complex [Eq. (3)], which reacts with dioxygen to produce superoxide anion [Eq. (4)]. The CuI complex reduced\u0026nbsp;..."},{"page_id":"PA87","page_number":"87","snippet_text":"... (40). Dizdaroglu et al . studied the oxidation of nucleobases of . FIG 8. Mechanism of C50 oxidation of DNA by activated Cu(phen) 2 . FIG . 11. \u003cb\u003eRedox\u003c/b\u003e events involved in the formation of. DNA OXIDATION BY COPPER AND MANGANESE COMPLEXES 87."},{"page_id":"PA89","page_number":"89","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e active 2 : 1 complex due to steric clash between N 2 N N 3 N N -NH2 -NH2 N N 2 - Clip - Phen 3 - Clip - Phen FIG . 9. Structure of 2- and 3 - Clip - Phen . II the ortho methyl groups ( which inhibits \u003cb\u003eredox\u003c/b\u003e cycling. DNA OXIDATION BY\u0026nbsp;..."},{"page_id":"PA90","page_number":"90","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e cycling through the square planar Cut complex ) ( 3,80 ) ; ( vi ) the new ligand must be as simple as possible and easy to prepare in large quantity if needed , so therefore must be symmetric . The first bridge tested was serinol\u0026nbsp;..."},{"page_id":"PA93","page_number":"93","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e potential couples were generally observed between +0.2 and +0.8 V ( 125,126 ) . These values are easily accessible in biological condi- tions and allow , as summarized in Fig . 11 , Cu1 species , derived from the reduction of\u0026nbsp;..."},{"page_id":"PA94","page_number":"94","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e events for the oxidation of. FIG . 11. \u003cb\u003eRedox\u003c/b\u003e events involved in the formation of di¡usible reactive oxygen species by CuII complexes in the presence of reductant and dioxygen. DNA radical formation by HOl. . FIG 14. Proposed\u0026nbsp;..."},{"page_id":"PA95","page_number":"95","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e events for the oxidation of DNA deoxyribose by an \u0026#39;\u0026#39;encaged\u0026#39;\u0026#39; hydroxyl radical, a proposed non-di¡usible active species formed in the pre- sence of a CuI complex and H2O2 . . FIG 13. Proposed \u003cb\u003eredox\u003c/b\u003e events for the oxidation of DNA\u0026nbsp;..."},{"page_id":"PA96","page_number":"96","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e events for the oxidation of DNA deoxyribose by a CuIII-oxo non-di¡usible active species formed in the presence of a CuI complex and H2O2 . . FIG 16. Proposed \u003cb\u003eredox\u003c/b\u003e events for the oxidation of DNA deoxyribose by a CuII- hydroperoxo\u0026nbsp;..."},{"page_id":"PA97","page_number":"97","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e events involving non - diffusible active species for the oxida- tion of DNA deoxyribose by a dinuclear Cut complex in the presence of dioxygen . ( a ) The \u0026quot; Cu - O - O - CuII \u0026quot; pathway . ( b ) Initiation of the \u0026quot; Cu - hydroperoxo\u0026nbsp;..."},{"page_id":"PA99","page_number":"99","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e active Cu1 complexes unable to oxidize DNA . III . Oxidative DNA Damage by Manganese Complexes The few examples of manganese complexes able to damage DNA by oxida- tive processes came from the intensive work on metal complexes\u0026nbsp;..."},{"page_id":"PA111","page_number":"111","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e potential of the guanine base of guanosine was measured at 1.29 V vs. NHE and is significantly lower ( 0.5V ) than that of the nearest nucleoside , adenosine ( 214 ) . However , depending on the DNA sequence , the guanine bases\u0026nbsp;..."},{"page_id":"PA122","page_number":"122","snippet_text":"... oxidative species that are two \u003cb\u003eredox\u003c/b\u003e equivalents above the initial state of the complex . These activated complexes are powerful oxidants not only in terms of electron transfer , but also in oxygen transfer reactions. 122 M. PITIÉ et al ."},{"page_id":"PA136","page_number":"136","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e properties , and their consequences on O2 reactivity including thermodynamic , kinetic , and bonding properties of derived copper - dioxygen adducts ( 19 ) . Inorganic model studies have shown that several different O2 binding\u0026nbsp;..."},{"page_id":"PA142","page_number":"142","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e potential of the copper(I) and copper(II) (60) complexes increase as the ligand increases in arm length. This e¡ect is understood as arising from the relative stability (i.e., formation constants) of the Cu(II) ions for a 5\u0026nbsp;..."},{"page_id":"PA143","page_number":"143","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e potential and ligand chelate ring size of derived copper(I) complexes (Fig. 10). B. ELECTRONIC EFFECTS IN TETRADENTATE LIGAND SYSTEMS More recently, we modi¢ed the TMPA ligand in terms of its electronic donating ability to the\u0026nbsp;..."},{"page_id":"PA162","page_number":"162","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e properties, and steric accessibility, all a¡ect the oxidative capability of the activated copper-O 2 complex. Here, we ¢rst highlight some initial observations from our group demonstrating reactivity di¡erences from end-on, and\u0026nbsp;..."},{"page_id":"PA176","page_number":"176","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e potentials of each [{Cu(R-MePY2)} 2 ]2 þ oxidant, seeking an understanding of the preferential ETPT and ET/PT pathways from a thermodynamic perspective. In CH2 O2 Cl2 , [{Cu(H-MePY2)} the low temperature (^808C) cyclic 2O2 ]2þ and\u0026nbsp;..."},{"page_id":"PA178","page_number":"178","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e potentials of the oxidant and / or the substrate involved . Finally , as substrate binding appears to be a key step in the oxidation reaction , it is probably more correct to say that ET oxidations by [ { Cu ( R - MePY2 ) } 2O2 ]\u0026nbsp;..."},{"page_id":"PA186","page_number":"186","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e organic cofactors , resulting from posttranslational modifications of endogenous amino acids ( 7 ) , as in galactose oxidase ( 8 ) and amine oxidase ( 2,9 ) , or additional distant copper centers , as in dopamine ẞ - hydroxylase\u0026nbsp;..."},{"page_id":"PA192","page_number":"192","snippet_text":"... spectroscopic properties in the +2 \u003cb\u003eredox\u003c/b\u003e state as type 1 (or blue) Cu,. SCHEME 2. The catecholase catalytic cycle of tyrosinase (adapted from (44)). FIG. 3. Structure of the active site of multicopper oxidases. 192 G. BATTAINI et al."},{"page_id":"PA193","page_number":"193","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e active Cu centers need to store reducing equivalents coming from four substrate molecules and transfer the electrons to dioxygen. From spectroscopic studies and fast kinetic experiments carried out on laccase it has been shown\u0026nbsp;..."},{"page_id":"PA198","page_number":"198","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e properties of the copper centers and this is, inter alia, an important parameter to take into account when the properties of the biomimetic complexes are consid- ered. For instance, aliphatic amine ligands are strong s-donors and\u0026nbsp;..."},{"page_id":"PA220","page_number":"220","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e potential of the two partners and the overlap between the orbitals involved, while the activation entropy, AS61⁄4 1⁄4 73(6) J mol 1 K 1 shows a negative value. The analysis of the activa- tion parameters for the second step, AH61\u0026nbsp;..."},{"page_id":"PA236","page_number":"236","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e - catalysts that could be used for the green and selective oxidation of alcohols . Copper - containing oxidases can be divided into enzymes with mono- nuclear copper - sites , dinuclear copper - sites , and enzymes with\u0026nbsp;..."},{"page_id":"PA243","page_number":"243","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e potential of ca. 0.8 V vs. NHE . Consequently , fungal laccases can easily oxidize TEMPO to the corresponding oxoammonium cation , since the oxidation potential of the latter , which was first measured by Golubev and co - workers\u0026nbsp;..."},{"page_id":"PA244","page_number":"244","snippet_text":"... \u003cb\u003eredox\u003c/b\u003e metal ion , one of the phenol ligands is most likely involved in the oxidative transformation . Indeed , in the active form of the biocatalyst , the equatorial plane is formed by two nitrogen atoms from two histidine imidazoles\u0026nbsp;..."},{"page_id":"PA284","page_number":"284","snippet_text":"... \u003cb\u003eRedox\u003c/b\u003e cycling 90 Reductants 80 , 98 , 176 NADH ( 2 - electron reductants ) 80 superoxide anion and thiol ( 1 - electron reductant ) 80 used for the activation of Cu II 80 Regioselectivity 42 , 67 Retention of configuration ( RC ) 42\u0026nbsp;...","page_url":"https://books.google.com.sg/books?id=UgNp8-wq-aAC\u0026pg=PA284\u0026vq=redox\u0026dq=subject:%22Science+Chemistry%22"},{"page_id":"PA286","page_number":"286","snippet_text":"... \u003cb\u003eRedox\u003c/b\u003e Enzymes and Model Systems : Properties , Structures , and Reactivity VOLUME 48 Cumulative Index for Volumes 1^47 VOLUME 49 Inorganic. Neil A. Law , M. Tyler Caudle , and Vincent L. Pecoraro Calcium - Binding Proteins Bryan E. Finn\u0026nbsp;...","page_url":"https://books.google.com.sg/books?id=UgNp8-wq-aAC\u0026pg=PA286\u0026vq=redox\u0026dq=subject:%22Science+Chemistry%22"},{"page_id":"PA288","page_number":"288","snippet_text":"... \u003cb\u003eRedox\u003c/b\u003e Chemistry and Functionalities of Conjugated Ferrocene Systems Hiroshi Nishihara New Aspects of Metal - Nucleobase Chemistry Andrew Houlton INDEX VOLUME 55 Dioxygen Activation by Transition Metal Complexes . Atom Transfer and Free\u0026nbsp;..."},{"page_id":"PA289","page_number":"289","snippet_text":"Homogeneous Biomimetic Oxidation Catalysis Rudi van Eldik, Jan Reedijk. \u003cb\u003eRedox\u003c/b\u003e Reactivity of Coordinated Ligands in Pentacyano ( L ) Ferrate Complexes José A. Olabe Carbonato Complexes : Models for Carbonic Anhydrase Achyuta N. Acharya\u0026nbsp;..."}],"search_query_escaped":"redox"},{});</script></div></div></div><script>(function() {var href = window.location.href;if (href.indexOf('?') !== -1) {var parameters = href.split('?')[1].split('&');for (var i = 0; i < parameters.length; i++) {var param = parameters[i].split('=');if (param[0] == 'focus') {var elem = document.getElementById(param[1]);if (elem) {elem.focus();}}}}})();</script>