Redox-Active Amino Acids in Biology
Author: ABELSON John N.Language: Anglais
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392 p. · 22.9x15.2 cm · Hardback
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.
* Among the redox-active prosthetic groups covered are:
* Topa quinones
* Pyrroloquinoline quinones
* Tryptophan tryptophylquinones
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.
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