Molecular Structure, Function, and Assembly of the ATP Synthases : International Seminar

Sangkot Marzuki

ISBN 10: 1461278821 / ISBN 13: 9781461278825

Editore: Springer, Springer, 2011

Riguardo questo articolo

Druck auf Anfrage Neuware - Printed after ordering - In recent years, the ATP synthase (H+ ATPase, FoFrATPase) has been the subject of intensive IDvestigations in many laboratories. The major reason for this lies in the fact that this enzyme complex catalyses one of the most important reactions in living cells, namely the synthesis of ATP utilizing the energy from an electrochemical transmembrane H+ gradient, generated by the cellular respiratory chain or by the light reactions of photosynthetic organisms. The mechanism by which the H+ motive force is utilized to drive the synthesis of ATP is one of the major unsolved problems in biochemistry. Thus, the fundamental information concerning the-molecular structure and the mechanism of assembly of the ATP synthase is of major significance in cell biology. A seminar/workshop on the Molecular Structure, Function and Assembly of the ATP synthases was held in April, 1987 at the East West Center, University of Hawaii, Honolulu, Hawaii, to promote exchange of information between laboratories actively engaged in the study of the A TP synthases, and to provide a forum for discussion and coordination of data derived from molecular, genetic and biochemical approaches used in different laboratories. This volume summarizes the result of the seminar/workshop, in the form of a collection of papers presented at the meeting, and provides an overvIew of current work in this rapidly progressing area of research.

Codice articolo 9781461278825

Dati bibliografici

• Titolo: Molecular Structure, Function, and Assembly of the ATP Synthases : International Seminar
• Editore: Springer, Springer
• Data di pubblicazione: 2011
• Lingua: Inglese
• ISBN 10: 1461278821
• ISBN 13: 9781461278825
• Rilegatura: Taschenbuch
• Condizione: Neu
• Dimensioni: 244 L x 170 A x 17 P (millimetri) 244 millimetri di larghezza per 170 millimetri di altezza per 17 millimetri di profondità
• Peso: 522 grammi

Descrizione articolo

Riassunto

In recent years, the ATP synthase (H+·ATPase, FoFrATPase) has been the subject of intensive IDvestigations in many laboratories. The major reason for this lies in the fact that this enzyme complex catalyses one of the most important reactions in living cells, namely the synthesis of ATP utilizing the energy from an electrochemical transmembrane H+ gradient, generated by the cellular respiratory chain or by the light reactions of photosynthetic organisms. The mechanism by which the H+ motive force is utilized to drive the synthesis of ATP is one of the major unsolved problems in biochemistry. Thus, the fundamental information concerning the-molecular structure and the mechanism of assembly of the ATP synthase is of major significance in cell biology. A seminar/workshop on the Molecular Structure, Function and Assembly of the ATP synthases was held in April, 1987 at the East·West Center, University of Hawaii, Honolulu, Hawaii, to promote exchange of information between laboratories actively engaged in the study of the A TP synthases, and to provide a forum for discussion and coordination of data derived from molecular, genetic and biochemical approaches used in different laboratories. This volume summarizes the result of the seminar/workshop, in the form of a collection of papers presented at the meeting, and provides an overvIew of current work in this rapidly progressing area of research.

Contenuti

Molecular Genetics of the ATP Synthase.- Gene Structure and Function of Thermophilic ATP Synthase.- Genetic Studies of F1-ATPase of Escherichia coli.- The Chloroplast Genes Encoding CF0 Subunits of ATP Synthase.- Expression and Evolution of the Chloroplast ATP Synthase Genes.- Structure and Expression of Genes Encoding Higher Plant Mitochondrial F1F0-ATPase Subunits.- Polypeptide Synthesis, Import and Assembly.- The Assembly of the F1F0-ATPase Complex in Escherichia coli.- Biochemical Analyses of oli1 and oli2 Gene Mutations Determining Primary Sequence Changes in Subunits 9 and 6 of Yeast ATP Synthase.- The Structure and Expression of a Human Gene for a Nuclear-Coded Mitochondrial Adenosine Triphosphate Synthase Beta Subunit.- Isolation of a cDNA Clone for the ? Subunit of the Chlamydomonas reinhardtii CF1.- Import and Assembly of the Mitochondrial ATP Synthase of Baker’s Yeast.- Assembly of Yeast Mitochondrial ATP Synthase Incorporating an Imported Version of an F0 Sector Subunit Normally Encoded within the Organelle.- Structure and Function of ATP Synthase.- Structure of the Escherichia coli ATP Synthase from Electron Microscopy Studies.- Monoclonal Antibodies as Probes of Assembly of the Mitochondrial ATP Synthase.- The Proton-ATPase of Chromaffin Granules and Synaptic Vesicles.- A H+-Translocating ATP Synthase in an Extremely Halophilic Archaebacterium.- The F0 Sector and Proton Motive Coupling.- Structure and Function of Mitochondrial Coupling Factor B (FB).- Subunit Arrangement in Bovine Mitochondrial H+-ATPase.- Interaction of Regulatory Subunits with the F1 Sector of ATP Synthase in Mitochondria.- The pKa Gate Mechanism for Protomotive Coupling: Effects of Internal Buffers on Initial Rates of ATP Synthesis.- ATP Synthesis Driven by Intramembranal Protons.- ATP Synthase Reaction Mechanisms.- Catalysis by Isomeric Forms of Covalently Labeled F1-ATPase.- Catalytic and Noncatalytic Nucleotide Binding Sites of F1-ATPases: Probes of Location, Structure and Function by use of 2-N3-ATP.- Interaction of Arylazido-?-Alanyl ATP with the ATPase Enzyme of Rhodospirilum rubrum Chromatophores.- Catalytic Cooperativity in F1-ATPase: Photoaffinity Labeling Studies with BzATP.- On the Number of Catalytic Sites in the F1-ATPase that Catalyze Steady State ATP Hydrolysis.- The Effects of Neutral Salts and Nucleotides on the Stability of Beef Heart Mitochondrial F1-ATPase.- Characterization of Nucleotide Binding Sites on Chloroplast Coupling Factor 1 (CF1): Effects of Nucleotide Triphosphate Formation by Isolated CF1.- A Hydrophobic Protein, Chargerin II, Purified from Rat Liver Mitochondria is Encoded in the Unidentified Reading Frame A6L of Mitochondrial DNA.- Contributors.