Redox-Active Amino Acids in BiologyEdited by
- Judith Klinman
- John Abelson
- Melvin Simon
General Description of the Volume:The role of low molecular weight cofactors (often vitamins) in enzyme catalysis has been discussed in many earlier volumes of Methods in Enzymology. Exciting new results indicate that redox-active prosthetic groups can also arise from pre-existing amino acid side chains in proteins. In this volume, methods are described for the detection and characterization of such prosthetic groups in a range of enzyme systems.General Description of the Series:The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.
Biochemists, molecular biologists, and biophysicists.
Methods in Enzymology
Hardbound, 415 Pages
Published: August 1995
Imprint: Academic Press
"This monograph in the Methods in Enzymology series provides an important framework for methods available for studies of redox amino acids. This book is high quality in terms of content, organization, and format."
Praise for the Volume, --DOODYS JOURNAL
"The Methods in Enzymology series represents the gold-standard."
Praise for the Series, --NEUROSCIENCE
"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."
--CHEMISTRY IN INDUSTRY
"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
- J.H. Waite, Precursors of Quinone-Tanning: Dopa-Containing Proteins.S.M. Janes and J.P. Klinman, Isolation of 2,4,5-Trihydroxyphenylalanine Quinone (Topa Quinone) from Copper Amine Oxidases.M. Palcic and S.M. Janes, Spectrophotometric Detection of Topa Quinone.M. Mure and J.P. Klinman, Model Studies of Topa Quinone: Synthesis and Characterization of Topa Quinone Derivatives.L.M. Sayre and Y. Lee, Catalytic Aerobic Deamination of Activated Primary Amines by a Model for the Quinone Cofactor of Mammalian Copper Amine Oxidases.C. Hartmann and D.M. Dooley, Detection of Reaction Intermediates in Topa Quinone Enzymes.G.W. Adams, P. Mayer, K.F. Medzihradszky, and A.L. Burlingame, Mass Spectrometric Studies of the Primary Sequence and Structure of Bovine Liver and Serum Amine Oxidase.D. Mu and J.P. Klinman, Cloning of Mammalian Topa Quinone-Containing Enzymes.H.M. Kagan and P. Cai, Isolation of Active Site Peptides of Lysyl Oxidase.D.M. Dooley and D.E. Brown, Resonance Raman Spectroscopy of Quinoproteins.R. Flackiger, M.A. Paz, and P.M. Gallop, Redox-Cycling Detection of Dialyzable Pyrroloquinoline Quinone (PQQ) and Quinoproteins.W.S. McIntire, TryptophanTryptophylquinone (TTQ) in Bacterial Amine Dehydrogenases.S. Itoh and Y. Ohshiro, Model Studies of Cofactor Tryptophan Tryptophylquinone (TTQ).V.L. Davidson, H.B. Brooks, M.E. Graichen, L.H. Jones, and Y.-L. Hyun, Detection of Intermediates in Tryptophan Tryptophylquinone (TTQ) Enzymes.F.S. Mathews, X-Ray Studies of Quinoproteins.M.E. Lidstrom, Genetics of Bacterial Quinoproteins.C.J. Unkefer, D.R. Houck, B.M. Britt, T.R. Sosnick, and J.L. Hanners, Biogenesis of Pyrrolquinoline Quinone from 13C-Labeled Tyrosine.N. Ito, P.F. Knowles, and S.E.V. Phillips, X-Ray Crystallographic Studies of Cofactors in Galactose Oxidase.J.W. Whittaker, Spectroscopic Studies of Galactose Oxidase.J.M. Bollinger, Jr.,W.H. Tong, N. Ravi, B.H. Huynh, D.E. Edmondson, and J. Stubbe, Use of Rapid Kinetics Methods to Study the Assembly of the Diferric-Tyrosyl Radical Cofactor of E. coli Ribonucleotide Reductase.B.A. Barry, Tyrosyl Radicals in Photosystem II.S.-T. Kim, P.F. Heelis, and A. Sancar, Role of Tryptophans in Substrate Binding and Catalysis by DNA Photolyase.J. Knappe and A.F.V. Wagner, Glycyl Free Radical in Pyruvate Formate-Lyase: Synthesis, Structure Characteristics, and Involvementin Catalysis.G.H. Reed and M.D. Ballinger, Characterization of a Radical Intermediate in the Lysine 2,3-Aminomutase Reaction.E.R. Stadtman, Role of Oxidized Amino Acids in Protein Breakdown and Stability.Author Index.Subject Index.