Download or read book Oxygen Intermediates of Mononuclear Non heme Iron Systems written by Andrea Decker and published by . This book was released on 2006 with total page 606 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book High valent Oxygen Intermediates of Mononuclear Non heme Iron Enzymes written by Shaun Di Hang Wong and published by . This book was released on 2012 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Mononuclear non-heme iron (NHFe) enzymes catalyze a wide variety of biologically-important reactions such as hydroxylation, halogenation, desaturation, ring closure, and electrophilic aromatic substitution. The key intermediate in the catalytic cycle is the S = 2 Fe(IV)=O species, capable of abstracting an H-atom from inert C--H bonds as strong as 106 kcal/mol. The Fe(IV)=O intermediate in enzymes is transient and difficult to trap; as such, stable synthetic analogs have proven invaluable for spectroscopic elucidation of the geometric/electronic structure of the Fe(IV)=O unit and how it is activated for reactivity. Such biomimetic Fe(IV)=O model complexes can be either intermediate-spin (S = 1) or high-spin (S = 2) in contrast to the S = 2 ground state of enzyme intermediates. For an S = 1 Fe(IV)=O species, the Fe--oxo [beta] [pi]*-frontier molecular orbital (FMO) [from the combination of Fe d(xz/yz) and oxo p(x/y)] is involved in H-atom abstraction, and this FMO requires a side-on approach ([pi]-attack) to achieve maximum overlap with the substrate C--H bond. Through magnetic circular dichroism (MCD) and nuclear vibrational resonance spectroscopy (NRVS) studies, the reactivity of the S = 1 Fe(IV)=O unit has been shown to be affected by the oxo contribution in the [pi]*-FMO, where a larger oxo contribution results in greater orbital overlap (with the substrate C--H) and higher reactivity; also, the [pi]-attack pathway results in steric clashes between substrate and ligand, giving a significant steric contribution to the energy of the reaction barrier. For an S = 2 Fe(IV)=O species, the Fe--oxo [alpha] [sigma]*-FMO [Fe d(z2) and oxo p(z)] is spin-polarized (exchange-stabilized) to an energy level comparable with its [pi]*-FMO, making it accessible as a second pathway ([sigma]-attack) for reactivity. In the S = 2 Fe(IV)=O model complex ligated by TMG3tren, this [sigma]*-FMO is active but is axially hindered by the ligand, again giving a large steric contribution to the reaction barrier; however, the intrinsic electronic reaction barriers of the S = 2 [sigma]*-FMO and the S = 1 [pi]*-FMO are comparable, suggesting they are similarly active in H-atom abstraction. Furthermore, MCD excited-state spectroscopy in combination with multiconfigurational calculations on the S = 2 model reveal two different [pi]-pathways for reactivity involving Fe(III)--oxyl[p(x), [pi]] character, in addition to the [sigma]-pathway involving Fe(III)--oxyl[p(z), [sigma]] character, showing that the S = 2 Fe(IV)=O unit is activated for both [pi] and [sigma] H-atom abstraction reactivities. Finally, the S = 2 enzyme intermediate for the halogenase SyrB2 was trapped and structurally characterized by NRVS, revealing two possible 5-coordinate trigonal bipyramidal candidates with the Fe--oxo vector oriented either perpendicular or parallel to the substrate C--H bond. Importantly, this difference in orientation leads to Fe(III)--OH products oriented efficiently for different rebound reactivities -- native halogenation in the case of perpendicular orientation and non-native hydroxylation in the case of parallel orientation.
Download or read book Iron containing Enzymes written by Sam P. De Visser and published by Royal Society of Chemistry. This book was released on 2011 with total page 463 pages. Available in PDF, EPUB and Kindle. Book excerpt: Mononuclear iron containing enzymes are important intermediates in bioprocesses and have potential in the industrial biosynthesis of specific products. This book features topical review chapters by leaders in this field and its various sub-disciplines.
Download or read book Characterization and Mechanistic Study of Oxygen iron Intermediates in Mononuclear Nonheme Model Systems written by Michael R. Bukowski and published by . This book was released on 2005 with total page 494 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Oxygen Activation by Mononuclear Non heme Iron Enzymes written by Jeffrey T Babicz and published by . This book was released on 2022 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: Non-heme iron (NHFe) enzymes are in critical in Nature, playing significant roles in bioremediation, the biosynthesis of natural products, DNA repair and human health. These metalloenzymes utilize an Fe cofactor to activate dioxygen for reaction with organic substrates in a wide variety of chemical transformations including: H-atom abstraction, hydroxylation, halogentation, aromatic ring cleavage, aliphatic ring expansion/formation, electrophilic aromatic substitution and sulfur oxygenation/oxidation. Elucidating the mechanisms of these diverse catalysts requires defining the geometric and electronic structure of key Fe-O2 intermediates along the reaction cycle. An ideal tool for the interrogation of these Fe-O2 intermediates is nuclear resonance vibrational spectroscopy (NRVS), a synchrotron-based technique that observes the vibrational side-bands of the Fe-57 Mossbauer transition, making it a site-selective probe of all normal modes containing Fe displacement. Interpretation and analysis of NRVS spectra by correlation to quantum mechanical simulations (via density functional theory), allows for assignment of Fe vibrations and crucially geometric structure. In this thesis, NRVS is applied to the Fe-O2 intermediates in the extradiol dioxygenase, homoprotocatechuate 2,3-dioxygenase (HPCD-HPCA-Int-1) and the intradiol dioxygenase, protocatechuate 3,4-dioxygenase (PCD-4FC-Int-1), the pre-Fe(IV)=O intermediate in the pterin-dependent hydroxylase, tryptophan hydroxylase, and intermediate Q in methane monooxygenase (included in the appendix), while the ETHE1 sulfur oxidase versus oxygenase and the alpha-KG-dependent DAOCS concerted versus sequential DAOCS mechanistic studies utilize a combination of spectroscopic methods.
Download or read book Activation of Dioxygen by a Mononuclear Nonheme Iron Complex Via Sequential Peroxo Oxo and Hydroxo Intermediates written by David Philip Goldberg and published by . This book was released on 2017 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: The activation of dioxygen by nonheme iron centers is of fundamental importance to biological and synthetic oxidation reactivity. Dioxygen activation by nonheme iron is often proposed to follow a sequence of steps involving initial O2 binding, reduction of O2 to form a peroxo species, and Ou2013O bond cleavage to produce a reactive high-valent FeIV(O) intermediate. Individual intermediates involved in these steps have been observed in both synthetic and enzymatic systems; however, the observation of multiple, sequentially formed Fe/oxygen intermediates is extremely rare. This presentation will discuss the reactivity of a dithiolate-ligated nonheme iron complex, FeII(Me3TACN)(S2SiMe2), with dioxygen to produce a peroxo(diiron) species, FeIII2(O2)(Me3TACN)2(S2SiMe2)2, which was characterized by UV-vis, Mu00f6ssbauer, resonance Raman (RR), and X-ray absorption spectroscopies. This peroxo(diiron) complex undergoes photochemically or thermally induced Ou2013O bond cleavage to generate an FeIV(O) complex, FeIV(O)(Me3TACN)(S2SiMe2), exhibiting a highly activated FeIV=O bond, as seen by RR and X-ray absorption spectroscopy. The FeIV(O) reacts with H-atom donors to produce an FeIII(OH) complex, FeIII(OH)(Me3TACN)(S2SiMe2), which could also be synthesized independently by addition of a one-electron oxidant followed by a hydroxide source to the FeII complex. The generation, stability, and spectroscopic characterization of each of these species will be discussed.
Download or read book Molecular Catalysts written by Lutz H. Gade and published by John Wiley & Sons. This book was released on 2014-06-30 with total page 632 pages. Available in PDF, EPUB and Kindle. Book excerpt: Highlighting the key aspects and latest advances in the rapidly developing field of molecular catalysis, this book covers new strategies to investigate reaction mechanisms, the enhancement of the catalysts' selectivity and efficiency, as well as the rational design of well-defined molecular catalysts. The interdisciplinary author team with an excellent reputation within the community discusses experimental and theoretical studies, along with examples of improved catalysts, and their application in organic synthesis, biocatalysis, and supported organometallic catalysis. As a result, readers will gain a deeper understanding of the catalytic transformations, allowing them to adapt the knowledge to their own investigations. With its ideal combination of fundamental and applied research, this is an essential reference for researchers and graduate students both in academic institutions and in the chemical industry. With a foreword by Nobel laureate Roald Hoffmann.
Download or read book Mononuclear Non heme Iron Dependent Enzymes Part B written by and published by Elsevier. This book was released on 2024-09-17 with total page 382 pages. Available in PDF, EPUB and Kindle. Book excerpt: Mononuclear Non-heme Iron Dependent Enzymes, Volume 703 PART B focuses on methods for studying, characterizing, and leveraging the chemistry of mononuclear non-heme iron dependent enzymes. Chapters in this new release include Photoreduction for Rieske oxygenase chemistry, Insights into the Mechanisms of Rieske Oxygenases from Studying the Unproductive Activation of Dioxygen, Non-heme iron and 2-oxoglutarate enzymes catalyze cyclopropane and azacyclopropane formations, Obtaining precise metrics of substrate positioning in Fe(II)/2OG dependent enzymes using Hyperfine Sublevel Correlation Spectroscopy, Xe-pressurization studies for revealing substrate-entrance tunnels, and much more. Additional chapters cover A tale of two dehydrogenases involved in NADH recycling, Rieske oxygenases and/or their partner reductase proteins, Expression, assay and inhibition of 9-cis-epoxycarotenoid dioxygenase (NCED) from Solanum lycopersicum and Zea mays, Biocatalysis and non-heme iron enzymes, In vitro analysis of the three-component Rieske oxygenase cumene dioxygenase from Pseudomonas fluorescens IP01, Structure and function of carbazole 1,9a-dioxygenase, Characterization of a Mononuclear Nonheme Iron-dependent Mono-oxygenase OzmD in Oxazinomycin Biosynthesis, and much more. Provides detailed articles regarding how to study the structures and mechanisms of mononuclear non-heme iron dependent enzymes Guides readers on how to use partner proteins in non-heme iron enzyme catalysis Includes strategies to employ mononuclear non-heme iron enzymes in biocatalytic applications
Download or read book Mononuclear Non heme Iron Dependent Enzymes written by and published by Elsevier. This book was released on 2024-09-01 with total page 348 pages. Available in PDF, EPUB and Kindle. Book excerpt: Mononuclear Non-heme Iron Dependent Enzymes, Volume 703 focuses on methods for studying, characterizing, and leveraging the chemistry of mononuclear non-heme iron dependent enzymes. Chapters in this new release include Photoreduction for Rieske oxygenase chemistry, Insights into the Mechanisms of Rieske Oxygenases from Studying the Unproductive Activation of Dioxygen, Non-heme iron and 2-oxoglutarate enzymes catalyze cyclopropane and azacyclopropane formations, Obtaining precise metrics of substrate positioning in Fe(II)/2OG dependent enzymes using Hyperfine Sublevel Correlation Spectroscopy, Xe-pressurization studies for revealing substrate-entrance tunnels, and much more. Additional chapters cover A tale of two dehydrogenases involved in NADH recycling, Rieske oxygenases and/or their partner reductase proteins, Expression, assay and inhibition of 9-cis-epoxycarotenoid dioxygenase (NCED) from Solanum lycopersicum and Zea mays, Biocatalysis and non-heme iron enzymes, In vitro analysis of the three-component Rieske oxygenase cumene dioxygenase from Pseudomonas fluorescens IP01, Structure and function of carbazole 1,9a-dioxygenase, Characterization of a Mononuclear Nonheme Iron-dependent Mono-oxygenase OzmD in Oxazinomycin Biosynthesis, and much more. Provides detailed articles regarding how to study the structures and mechanisms of mononuclear non-heme iron dependent enzymes Guides readers on how to use partner proteins in non-heme iron enzyme catalysis Includes strategies to employ mononuclear non-heme iron enzymes in biocatalytic applications
Download or read book Physical Inorganic Chemistry written by Andreja Bakac and published by John Wiley & Sons. This book was released on 2010-04-22 with total page 620 pages. Available in PDF, EPUB and Kindle. Book excerpt: This go-to text provides information and insight into physical inorganic chemistry essential to our understanding of chemical reactions on the molecular level. One of the only books in the field of inorganic physical chemistry with an emphasis on mechanisms, it features contributors at the forefront of research in their particular fields. This essential text discusses the latest developments in a number of topics currently among the most debated and researched in the world of chemistry, related to the future of solar energy, hydrogen energy, biorenewables, catalysis, environment, atmosphere, and human health.
Download or read book 2 Oxoglutarate Dependent Oxygenases written by Christopher J Schofield and published by Royal Society of Chemistry. This book was released on 2015-05-06 with total page 508 pages. Available in PDF, EPUB and Kindle. Book excerpt: Since the discovery of the first examples of 2-oxoglutarate-dependent oxygenase-catalysed reactions in the 1960s, a remarkably broad diversity of alternate reactions and substrates has been revealed, and extensive advances have been achieved in our understanding of the structures and catalytic mechanisms. These enzymes are important agrochemical targets and are being pursued as therapeutic targets for a wide range of diseases including cancer and anemia. This book provides a central source of information that summarizes the key features of the essential group of 2-oxoglutarate-dependent dioxygenases and related enzymes. Given the numerous recent advances and biomedical interest in the field, this book aims to unite the latest research for those already working in the field as well as to provide an introduction for those newly approaching the topic, and for those interested in translating the basic science into medicinal and agricultural benefits. The book begins with four broad chapters that highlight critical aspects, including an overview of possible catalytic reactions, structures and mechanisms. The following seventeen chapters focus on carefully selected topics, each written by leading experts in the area. Readers will find explanations of rapidly evolving research, from the chemistry of isopenicillin N synthase to the oxidation mechanism of 5-methylcytosine in DNA by ten-eleven-translocase oxygenases.
Download or read book Advances in Biological Science Research written by Surya Nandan Meena and published by Academic Press. This book was released on 2019-05-17 with total page 580 pages. Available in PDF, EPUB and Kindle. Book excerpt: Advances in Biological Science Research: A Practical Approach provides discussions on diverse research topics and methods in the biological sciences in a single platform. This book provides the latest technologies, advanced methods, and untapped research areas involved in diverse fields of biological science research such as bioinformatics, proteomics, microbiology, medicinal chemistry, and marine science. Each chapter is written by renowned researchers in their respective fields of biosciences and includes future advancements in life science research. Discusses various research topics and methods in the biological sciences in a single platform Comprises the latest updates in advanced research techniques, protocols, and methods in biological sciences Incorporates the fundamentals, advanced instruments, and applications of life science experiments Offers troubleshooting for many common problems faced while performing research experiments
Download or read book Advances in Enzymology and Related Areas of Molecular Biology Volume 73 Part A written by Daniel L. Purich and published by John Wiley & Sons. This book was released on 1999-04-22 with total page 304 pages. Available in PDF, EPUB and Kindle. Book excerpt: Biological catalysis plays a dominant role both in fermentation and industrial process chemistry. This collection of chapters, written by a well-known biochemist and enzymologist, should serve as an invaluable reference to those investigators seeking to optimize the application of enzymatic catalysis for commercial purposes.
Download or read book Progress in Inorganic Chemistry Volume 50 written by Kenneth D. Karlin and published by John Wiley & Sons. This book was released on 2004-03-24 with total page 641 pages. Available in PDF, EPUB and Kindle. Book excerpt: This series provides inorganic chemists and materials scientists with a forum for critical, authoritative evaluations of advances in every area of the discipline. Volume 50 continues to report recent advances with a significant, up-to-date selection of contributions on topics such as the following: Structural and mechanistic investigations in asymmetric copper; Catalyzed reactions; Phenoxyl radical complexes; Synthesis of large pore zeolites and molecular sieves; Inorganic nanoclusters with fullerene-like structure and nanotubes
Download or read book X ray Absorption Spectroscopy of Heme and Non heme Iron written by Samuel Aaron Wilson and published by . This book was released on 2012 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: In biological systems dioxygen serves two essential functions, one as a terminal electron acceptor, and two as a biosynthetic agent. The latter role will be primarily the focus of this thesis, which will look at the role of dioxygen in specific mononuclear iron metalloenzyme and biomimetic model systems. During enzymatic turnover, the use of dioxygen as a biosynthetic agent involves the binding of dioxygen and the formation of one or more iron-peroxo (Fe-OO) or hydroperoxo (Fe-OOH) intermediates. This is followed by the controlled cleavage of the oxygen-oxygen double bond, a highly energetically favorable and exothermic process, to form a high-valent iron-oxo intermediate. For many enzymatic systems, these iron-oxygen species and high-valent intermediates are represent a significant obstacle as they are often difficult to trap and isolate in pure form, making them very challenging to study. Thus, biomimetic model complexes offer an excellent way to understand the mechanisms for reactivity and how the enzyme may tune the ligand environment around the iron center in order to govern the electronic structure of many of these key intermediate species. Chapter 1 will introduce the fields of iron non-heme enzymes, heme enzymes, and biomimetic model studies that play a key role in understanding the enzyme systems that they represent. Chapter 1 will also introduce the methodology of X-ray absorption spectroscopy, a specialized spectroscopic technique that has been invaluable in understanding these difficult to study systems. Chapter 2 looks at the enzyme tyrosine hydroxylase, a pterin-dependent non-heme iron enzyme that utilizes dioxygen to catalyze the hydroxylation of L-tyr to L-DOPA in the rate-limiting step of catecholamine neurotransmitter biosynthesis. X-ray absorption spectroscopy (XAS) and variable-temperature-variable-field magnetic circular dichroism (VTVH MCD) spectroscopy are combined with single-turnover kinetic experiments to investigate the geometric and electronic structure of the wild-type tyrosine hydroxylase and two mutants, S395A and E332A, and their interactions with substrates. This research showns that all three forms of tyrosine hydroxylase undergo 6-coordinate (6C) → 5-coordinate (5C) conversion with tyr + pterin, consistent with the general mechanistic strategy established for O2-activating non-heme iron enzymes. When the FeII site is 6C, the two-electron reduction of O2 to peroxide by FeII and pterin is favored over individual one-electron reactions demonstrating that both a 5C FeII and a redox-active pterin are required for coupled O2 reaction. When the FeII is 5C, the O2 reaction is accelerated by at least 2 orders of magnitude. Comparison of the kinetics of wild-type tyrosine hydroxylase, which produces FeIV=O + 4a-OH-pterin, and the E332A mutant, which does not, shows that the E332 residue plays an important role in directing the protonation of the bridged FeII-OO-pterin intermediate in wild-type to productively form the FeIV=O intermediate, which is responsible for the hydroxylation of L-tyr to L-DOPA. Chapter 3 uses a combination of nuclear resonance vibrational spectroscopy (NRVS) and extended X-ray absorption fine structure spectroscopy (EXAFS) to define the natures of ferric (FeIIIBLM) and activated bleomycin (ABLM), an important glycopeptide anticancer drug capable of effecting single- and double-strand DNA cleavage, as (BLM)FeIII-OH and (BLM)FeIII([eta]1-OOH) species, respectively. These spectroscopically defined species are then used in a series of density functional theory (DFT) calculations to show that the direct H-atom abstraction by ABLM is the most thermodynamically favored reaction pathway. Chapter 4 reports the first high-resolution x-ray crystal structure of an side-on ferric peroxide species in a non-heme iron biomimetic complex, [FeIII(OO)(TMC)]+, and a series of spectroscopic studies which looks at the pathway of interconversion from a iron(III)-peroxo complex to a iron(III)-hydroperoxo complex, followed by the homolytic O-O bond cleavage to an iron(IV)-oxo intermediate species. This work is followed by a series of reactivity studies that show that the iron(III)-hydroperoxo complex is the most reactive of the three in the deformylation of aldehydes, and has a similar reactivity to the iron(IV)--oxo complex in the C--H bond activation of alkylaromatics. These three species represent the three most biologically relevant iron-oxygen intermediates, and have all been synthesized utilizing the same macrocyclic ligand, which has allowed for the elucidation of key differences at the iron center and its bonding interactions with dioxygen, while the ligand environment remains fixed. Chapter 5 focuses in more detail on the high-valent FeIV=O species with the spectroscopic characterization of a new iron-oxo complex [FeIV=O(BQEN)]2+. This non-heme iron(IV)-oxo complex is shown to activate the C-H bonds of both alkanes and alcohols via a hydrogen-atom (H-atom) abstraction mechanism. This work also presents evidence for the formation of an additional high-valent iron-oxo intermediate species, [FeV=O(BQEN)]3+, which exhibits high reactivity in oxidation reactions and fast oxygen exchange with H218O. This FeV=O species is proposed as a possible active oxidant in the catalytic oxidation of alkanes and alcohols. Chapter 6 takes a more detailed look at the role of the equatorial ligand in the tuning in the iron-oxo unit by comparing the reactivity differences between two S = 1 non-heme iron-oxo species, [FeIV=O(TBC)(CH3CN)]2+ and [FeIV=O(TMC)(CH3CN)]2+. TBC, 1,4,8,11-tetrabenzyl-1,4,8,11-tetraazacyclotetradecane, is a equatorially constrained cyclam ligand which exhibits a greater than two orders of magnitude reactivity increase over TMC for both H-atom abstraction and oxo-transfer reactions. In this study, the S = 1 ground states of [FeIV=O(TBC)(CH3CN)]2+ and [FeIV=O(TMC)(CH3CN)]2+ are first structurally defined using XAS. Next, this structural information is utilized in a series of DFT calculations to look at what structural differences are responsible for the reactivity differences between these two very similar complexes and the mechanistic reactivity differences between the S = 1 and S = 2 surface for the biologically relevant H-atom abstraction and oxo-transfer reactions. Chapter 7 considers the electronic structure of the Fe--O2 bond in oxy-hemoglobin and oxy-myoglobin which is a long-standing issue in the field of bioinorganic chemistry. Here, spectroscopic studies have been complicated by the highly delocalized electronic structure of the porphyrin and calculations require interpretation of multi-determinant wavefunctions of a highly covalent site. Iron L-edge X-ray absorption spectroscopy (XAS) is used with a valence bond configuration interaction (VBCI) multiplet model to directly probe the electronic structure of the iron in the biomimetic FeO2 heme complex [Fe(pfp)(1-MeIm)O2] (pfp = meso-tetra([alpha], [alpha], [alpha], [alpha]-o-pivalamidophenyl)porphyrin). This method allows separate estimates of [sigma]-donor, [pi]-donor, and [pi]-acceptor interactions through ligand to metal charge transfer (LMCT) and metal to ligand charge transfer (MLCT) mixing pathways. The L-edge spectrum of [Fe(pfp)(1-MeIm)O2] is further compared to those of [FeII(pfp)(1-MeIm)2], [FeII(pfp)], and [FeIII(tpp)(ImH)2]+ (tpp = meso-tetraphenylporphyrin) which have FeII S = 0, FeII S = 1 and FeIII S = 1/2 ground states, respectively. These serve as the expected references for the three contributions to the ground state of oxy-pfp. This FeO2 S = 0 site is found to have significant [sigma]-donation and a strong [pi]-interaction of the O2 with the iron.
Download or read book Iron Porphyrins written by A. B. P. Lever and published by Wiley-VCH. This book was released on 1989-03-31 with total page 322 pages. Available in PDF, EPUB and Kindle. Book excerpt: Porphyrins play a vital role in many biological functions including oxygen transport, electron transfer and catalyzing the incorporation of oxygen into other molecules. This current survey discusses the use of modern physical techniques to probe porphyrin structure and function. The authors review the data available through a particular technique and show what can be learned therefrom about the (electronic) structure and function of biologically important porphyrins. The techniques include magnetic circular dichroism, X-ray absorption fine structure (EXAFS) and Mössbauer spectroscopies. All contributors are well known in their respective fields, enjoying world-wide reputation.
Download or read book Oxygen Atom Transfer Reactions written by Robert Bakhtchadjian and published by Bentham Science Publishers. This book was released on 2023-01-11 with total page 137 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book introduces readers to the fundamentals of oxygen atom transfer reactions. It also gives mechanistic insights into the redox processes occurring through the oxygen atom transfer reactions. It also includes information about catalytic activation of oxygen through enzymes and oxo-metallic complexes. All topics are explored in separate chapters. Key features: - reviews the basic mechanisms in redox processes involving oxo-atom transfer reactions. - presents progress in the biomimetic activation of dioxygen related to the catalytic oxidations by synthetic metal organic complexes. - covers an important class of metal-organic compounds - nickel-oxygen species - generated in catalytic oxidation processes as oxygen atom transfer agents. - explains the mechanistic aspects of the heterogeneous photochemical redox processes via oxo-atom transfer reactions - provides references for further reading It is a reference for both professional scientists in the fields of chemistry, biology and applied sciences, and for graduate and undergraduate students interested in understanding reaction mechanisms involving oxygen.
