There are many mononuclear iron containing enzymes in nature that utilize molecular oxygen and transfer one or both oxygen atoms of O2 to substrates. These enzymes catalyze many processes including the biosynthesis of hormones, the metabolism of drugs, DNA and RNA base repair and, the biosynthesis of antibiotics. Therefore, mononuclear iron containing enzymes are important intermediates in bioprocesses and have great potential in the commercial biosynthesis of specific products since they often catalyze reactions regioselectively or stereospecifically. Understanding their mechanism and function is important and will assist in searches for commercial exploitation. In recent years, advances in experimental as well as theoretical methodologies have made it possible to study the mechanism and function of these enzymes and much information on their properties has been gained. This book highlighting recent developments in the field is, therefore, a timely addition to the literature and will interest a broad readership in the fields of biochemistry, inorganic chemistry and computational chemistry. The Editors, leaders in the field of nonheme and heme iron containing monoxygenases, have filled the book with topical review chapters by leaders in the various sub-disciplines.
Зміст
Nonheme iron(IV)-oxo oxidants in enzymes: Spectroscopic properties and reactivity patterns; Heme iron(IV)-oxo oxidants in enzymes: Spectroscopic properties and reactivity patterns; Mechanism and function of taurine/ -ketoglutarate dioxygenase enzymes, an update; Mechanism and function of cysteine dioxygenase enzymes; Mechanism and function of heme peroxidase enzymes; Mechanism and function of cytochrome P450 enzymes; Biomimetic studies of mononuclear nonheme iron containing oxidants; Biomimetic studies of mononuclear porphyrin containing oxidants; Density functional calibration studies on iron-containing systems; Density functional theory studies on isomerisation reactions catalyzed by cytochrome P450 enzymes; Quantum mechanics/molecular mechanics studies of peroxidase enzymes; Theoretical modelling of nonheme iron containing oxidants
Про автора
The editors (SP de Visser and D Kumar) have been involved in studies of enzymatic systems such as heme enzymes like the cytochromes P450, peroxidases and catalases as well as on nonheme enzyme systems. These studies are at the forefront of chemistry and focus on short-lived species in enzymes and biomimetic complexes. Thus, for instance, the active oxidant of P450 enzymes is elusive and experimental studies gave conflicting results regarding what the active oxidant was. The studies of de Visser and Kumar and co-workers established what the active species of these enzymes is and ruled out many suggested alternative oxidants. They established a two-state-reactivity scenario for heme and nonheme iron(IV)-oxo oxidants that masquerades as multiple oxidants. Further studies established reaction mechanisms for the production of (unwanted) by-products and showed how these can be prevented. Recent collaborative work of de Visser and Kumar established a general trend for substrate hydroxylation reactions by the cytochromes P450 and explained the mechanism via a valence bond curve crossing model. De Visser and Kumar have published more than 100 scientific publications in high-impact journals and as a consequence are regular speakers and scientific meetings and conferences.
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