Mechanisms of Metallocenter Assembly
Published on 28. December 1995
Book
Hardback
XIV, 267 pages
978-0-471-18632-8 (ISBN)
Description
'Mechansisms of Metallocenter Assembly' summarizes the general principles and mechanisms involved in protein metallocenter assembly and illustrates these themes with specific examples. It provides a mechanistic framework for understanding how metals are incorporated into proteins, as well as systematic analysis of the various options available to the cell for controlling metal incorporation. The authors discuss the importance of metallocenter assembly in the activation of several enzymes and selected structural proteins. The possible reasons why expression of the structural gene is not enough to obtain a functional metalloprotein are also well covered. It is currently the only book that brings together experimental findings previously scattered in the literature on the mechanisms of metal incorporation into proteins.
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Content
General Principles and Mechanisms of Metallocenter Assembly (R. Hausinger); In Vitro Metal Ion Incorporation into Nonheme Diiron Proteins: Hemerythrin, Myohemerythrin, and Rubrerythrin (D. Kurtz); Generation of Calcium-Binding Sites in Proteins by Formation of gamma; -Carboxyglutamic Acid and beta;-Hydroxyaspartic Acid/ beta;-Hydroxyasparagine (T. Drakenberg, et al. ); Ferrochelatase (H. Dailey); Cobalt Insertion During Coenzyme B12 Biosynthesis (F. Blanche, et al. ); Developments in the Analysis of Nitrogenase FeMo-Cofactor Biosynthesis (S. Muchmore, et al. ); FeS Cluster Assembly by Rhodanese: A Regulated Process?(M. Volini); Nickel Incorporation into Urease (M. Moncrief R. Hausinger); Nickel Incorporation into Hydrogenases (T. Maier A. B?ck); Metal-Center Assembly of the Bacterial Multicopper Enzyme, Nitrous Oxide Reductase (W. Zumft P. Kroneck); Role of MelCI as a Chaperone for Streptomyces Tyrosinase Copper Assembly (Y. Lee); Role of Metallothionein in Intracellular Metal Metabolism and in Activation of Copper- and Zinc-Dependent Proteins (M. Brouwer); Index.