de Visser / Kumar Iron-Containing Enzymes

Versatile Catalysts of Hydroxylation Reactions in Nature
1. Auflage 2011
ISBN: 978-1-84973-298-7
Verlag: Royal Society of Chemistry
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)

E-Book, Englisch, 462 Seiten

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.

Autoren/Hrsg.

de Visser, Samuel P

Kumar, Devesh

Fachgebiete

• Naturwissenschaften Chemie Organische Chemie Organometallchemie
• Naturwissenschaften Chemie Physikalische Chemie Chemische Reaktionen, Katalyse

Inhaltsverzeichnis

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

Über Autor(innen)

de Visser, Samuel P
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.

Dr. Sam P. de Visser is based at the Manchester Interdisciplinary Biocenter and School of Chemical Engineering and Analytical Science in Manchester, UK. His research interests include the study of enzyme function and mechanism using theoretical chemistry techniques and the investigation of mononuclear and binuclear dimetal oxidants of substrate monoxygenation, dioxygenation and dehydrogenation. Dr Visser gained his M.Sc. and Ph.D from the University of Amsterdam in The Netherlands. His postdoctoral research was at King's College London and then the Hebrew University of Jerusalem. He has written several review articles and numerous research papers and has acted as a regular reviewer for numerous research journals. He also Guest Edited a special issue of the Journal of Physical Chemistry - A on "Sason Shaik Festschrift". He is a member of a number of scholarly societies and the winner of the Ramsay Memorial Fellowship of the Royal Netherlands Academy of Arts and Sciences (1997) and the Lise Meitner Minerva Junior Award from the Israel Chemical Society (2003). Dr. Devesh Kumar his based at the Max-Planck-Institut f³r Kohlenforschung, Germany. His research interests include studies of the reactivity of organic substrates with metalloenzymes or biomimetic catalysts and Simulations of intermolecular interactions in mesogens and biological molecules. Dr Kumar obtained is M.Sc. and Ph.D from Gorakhpur University in India. His postdoctoral research, before joining the The Max-Planck-Institut f³r Kohlenforschung, was at Nagarjuna University in India and The Hebrew University of Jerusalem. He has written several review articles and numerous research papers and has acted as a regular reviewer for numerous research journals. He has also delivered several important lectures and is a member of the Indian Biophysics Society. Devesh Kumar is Assistant Editor of Nanoscale Research Letters and has Guest Edited two special issues of the Journal of Physical Chemistry - A.