4 edition of Oxygenases and model systems found in the catalog.
Includes bibliographical references and index.
|Statement||edited by Takuzo Funabiki.|
|Series||Catalysis by metal complexes ;, v. 19|
|LC Classifications||QP603.O85 O875 1997|
|The Physical Object|
|Pagination||xi, 393 p. :|
|Number of Pages||393|
|LC Control Number||96035768|
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An up-to-date clarification of structures around active centres of heme- and nonheme-oxygenases is given with reference to the design of model complexes.
Various contributions also discuss in detail the formation, structure and reactivity of metal-oxygen and metal-substrate species in both enzyme and model systems. This volume contains 8 chapters written by leading researchers which together present an overview of di- and mono-oxygenases and their model systems from the point of.
This volume contains 8 chapters written by leading researchers which together present an overview of di- and mono-oxygenases and their model systems An up-to-date clarification Oxygenases and model systems book structures around active centres of heme- and nonheme-oxygenases is given with reference to the design of model complexes.
9 Model Oxygenases and Theoretical Considerations on the Activation of Oxygen I. Introduction II. General Physicochemical Considerations on Reaction Mechanisms Involving Free Oxygen III. General Phenomena Involving Free Oxygen IV.
Reaction Mechanisms in Biological and Model Oxidase Systems References 10 Cytochrome Oxidase I. Introduction Edition: 1. Prior to the discovery of oxygenases, it had long been generally believed that in biological systems either electrons or atoms are transferred and molecular oxygen serves as its ultimate acceptor, resulting in the production of H 2 O, H 2 O 2, or sometimes superoxide.
Book Review; Published: May Oxygenases and model systems. Edited by T. Funabiki Catalysis by Metal Complexes, Vol Editors R. Ugo and B.R. James, Kluwer. Hector R. Wong, in NeuroImmune Biology, 2 HAEM OXYGENASE. Haem oxygenase (HO) is responsible for catalyzing the first and rate-limiting step in the degradation of haem to bilirubin [1,2].It exists as three isoforms: HO-1, -2, and HO-1 is a 32 kDa protein that is highly inducible by a variety of cellular stressors and stimuli, including haem, nitric oxide, cytokines, heavy metals.
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