書誌事項

Light reaction path of photosynthesis

edited by Francis K. Fong ; with contributions by G.S. Beddard ... [et al.]

(Molecular biology, biochemistry and biophysics, v. 35)

Springer-Verlag, 1982

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注記

Bibliography: p. 340

Includes indexes

収録内容

  • Free energy change for quantum storage in photosynthesis / F.K. Fong
  • Phycobiliproteins, molecular aspects of photosynthetic antenna system / H. Scheer
  • Structure and excitation dynamics of light-harvesting protein complexes / G.S. Beddard, R.J. Cogdell
  • Photooxidation of the reaction center chlorophylls and structural properties of photosynthetic reaction centers / A.J. Hoff
  • Triplet state and chlorophylls / H. Levanon and J.R. Norris
  • The chlorophyll triplet state and the structure of chlorophyll aggregates / R.H. Clarke
  • Synthetic approaches to photoreaction center structure and function / M.R. Wasielewski
  • Light path of carbon reduction in photosynthesis / F.K. Fong

内容説明・目次

内容説明

This monograph deals with the light reaction pathway in photosynthesis. The photophysico-chemical events are presented in the order of their occurrence, beginning with the collection of sunlight by antenna systems, ending with the reduction of CO to carbohydrates. Relationships between the structural 2 properties and kinetic effects of primary and secondary events spanning time 12 domains in the range 1O- _ls are explored. Photosynthesis is examined in terms of a light-induced redistribution of reaction intermediates common to the biosynthesis and metabolic degradation of carbohydrates. The experimental procedures and results reviewed in the book are repre- sentative of developments in instrumental methods and conceptual formula- tions in this area during the past decade. In particular, picosecond spectroscopy, time-resolved and magnetic resonance techniques, along with structural and photoelectrochemical models of photosynthesis, have provided clues for the molecular mechanisms of energy migration from the antenna systems to the reaction centers, and of succeeding stages of photochemical events leading to the carbon-reduction cycle. The preparation of this monograph resulted from the efforts of workers in distantly separated institutions. The writer gratefully acknowledges the responsive collaboration of the contributing authors and members of the Springer editorial staff that made possible completion of the manuscript.

目次

1: Free Energy Change for Quantum Storage in Photosynthesis.- 1 Introduction.- 2 Definition of the Primary Photochemical Reaction.- 3 Photopotential, Photooverpotential and Free Energy Change for Quantum Storage in Photosynthesis.- 4 Outline of this Book.- References.- 2: Phycobiliproteins: Molecular Aspects of a Photosynthetic Antenna System.- 1 Introduction.- 2 Morphology.- 3 Energy Transfer.- 4 Chromophore Structure.- 4.1 Chromophores Cleaved from Biliproteins.- 4.2 Chromophores Bound to the Protein.- 5 Noncovalent Protein Chromophore Interactions.- 5.1 Topology of the Chromophore.- 5.2 Conformational Mobility.- 6 The Proteins.- 7 Biosynthesis.- 8 Concluding Remarks.- Notes Added in Proof.- References.- 3: Structure and Excitation Dynamics of Light-harvesting Protein Complexes.- 1 Introduction.- 1.1 General Discussion of Excitation Migration.- 1.2 Coherence.- 2 Experimental Methods.- 2.1 Streak Camera and Neodymium Laser.- 2.2 Single Photon Counting.- 3 Excited State Annihilation.- 4 Anaerobic Photosynthetic Bacteria.- 4.1 The B800-850 Light-harvesting Pigment-Protein Complex Isolated Isolated from Rps. sphaeroides.- 4.2 Kinetic Studies.- 4.3 The Water-soluble Bchl-a Antenna Complex from P. aestuarii, Strain 2K.- 5 Lower Algae.- 5.1 The Perdinin-Chl a Protein from Glenodinium.- 5.2 The Phycobiliproteins of the Red Algae.- 5.3 Kinetic Studies.- 6 Antenna Pigment-Protein Complexes from Higher Plants.- References.- 4: Photooxidation of the Reaction Center Chlorophylls and Structural Properties of Photosynthetic Reaction Centers.- Abbreviations and Symbols.- 1 Introduction.- 1.1 Energetics of Photosynthesis.- 1.2 Chlorophylls, Quinones and Related Molecules.- 2 The Photosystem of Purple Bacteria.- 2.1 Optical Investigations.- 2.1.1 Absorption Difference Spectroscopy.- 2.1.2 Spectroscopic Nomenclature of Bchl.- 2.1.3 Circular Dichroism.- 2.1.4 Linear Dichroism.- 2.1.5 Nano- and Picosecond Spectroscopy.- 2.2 ESR and ENDOR.- 2.2.1 Characteristics of the ESR Signal of P860+.- 2.2.2 ENDOR of the Primary Donor.- 2.2.3 ESR and ENDOR of the Reduced Intermediary Acceptor, I?.- 2.3 The Triplet State of the Primary Donor.- 3 The Plant Photosystems.- 3.1 Optical Investigations of the Primary Donor of Photosystems 1 and 2.- 3.1.1 Absorption Difference Spectroscopy of P700.- 3.1.2 Absorption Difference Spectroscopy of P680.- 3.1.3 Circular and Linear Dichroism of Photosystems 1 and 2.- 3.2 ESR and ENDOR.- 3.2.1 P700+.- 3.2.2 P680+.- 3.3 The Intermediary Acceptors of Photosystems 1 and 2.- 3.3.1 Photosystem 1.- 3.3.2 Photosystem 2.- 3.3.3 Triplet States.- 4 Structure of the Bacterial Primary Donor-Acceptor Complex.- 4.1 Electron Transfer Rates.- 4.2 Configuration of Primary Reactants.- References.- Notes Added in Proof (In Connection with Chapter 8).- 5: Triplet State and Chlorophylls.- Abbreviations.- 1 Introduction.- 2 Optical-Magnetic Resonance Spectroscopy.- 2.1 Triplet Detection. Zero Field Experiments.- 2.2 The Triplet State and the EPR Experiment.- 2.3 The Triplet Yield vs Magnetic Field.- 2.4 Triplet Photochemistry. The CIDEP Method.- 2.4.1 What is CIDEP?.- 2.4.2 Triplet Precursor vs Triplet Mechanism.- 2.4.3 The Triplet Mechanism.- 2.4.4 The Radical Pair Mechanism: ST+-1: Free Energy Change for Quantum Storage in Photosynthesis.- 1 Introduction.- 2 Definition of the Primary Photochemical Reaction.- 3 Photopotential, Photooverpotential and Free Energy Change for Quantum Storage in Photosynthesis.- 4 Outline of this Book.- References.- 2: Phycobiliproteins: Molecular Aspects of a Photosynthetic Antenna System.- 1 Introduction.- 2 Morphology.- 3 Energy Transfer.- 4 Chromophore Structure.- 4.1 Chromophores Cleaved from Biliproteins.- 4.2 Chromophores Bound to the Protein.- 5 Noncovalent Protein Chromophore Interactions.- 5.1 Topology of the Chromophore.- 5.2 Conformational Mobility.- 6 The Proteins.- 7 Biosynthesis.- 8 Concluding Remarks.- Notes Added in Proof.- References.- 3: Structure and Excitation Dynamics of Light-harvesting Protein Complexes.- 1 Introduction.- 1.1 General Discussion of Excitation Migration.- 1.2 Coherence.- 2 Experimental Methods.- 2.1 Streak Camera and Neodymium Laser.- 2.2 Single Photon Counting.- 3 Excited State Annihilation.- 4 Anaerobic Photosynthetic Bacteria.- 4.1 The B800-850 Light-harvesting Pigment-Protein Complex Isolated Isolated from Rps. sphaeroides.- 4.2 Kinetic Studies.- 4.3 The Water-soluble Bchl-a Antenna Complex from P. aestuarii, Strain 2K.- 5 Lower Algae.- 5.1 The Perdinin-Chl a Protein from Glenodinium.- 5.2 The Phycobiliproteins of the Red Algae.- 5.3 Kinetic Studies.- 6 Antenna Pigment-Protein Complexes from Higher Plants.- References.- 4: Photooxidation of the Reaction Center Chlorophylls and Structural Properties of Photosynthetic Reaction Centers.- Abbreviations and Symbols.- 1 Introduction.- 1.1 Energetics of Photosynthesis.- 1.2 Chlorophylls, Quinones and Related Molecules.- 2 The Photosystem of Purple Bacteria.- 2.1 Optical Investigations.- 2.1.1 Absorption Difference Spectroscopy.- 2.1.2 Spectroscopic Nomenclature of Bchl.- 2.1.3 Circular Dichroism.- 2.1.4 Linear Dichroism.- 2.1.5 Nano- and Picosecond Spectroscopy.- 2.2 ESR and ENDOR.- 2.2.1 Characteristics of the ESR Signal of P860+.- 2.2.2 ENDOR of the Primary Donor.- 2.2.3 ESR and ENDOR of the Reduced Intermediary Acceptor, I?.- 2.3 The Triplet State of the Primary Donor.- 3 The Plant Photosystems.- 3.1 Optical Investigations of the Primary Donor of Photosystems 1 and 2.- 3.1.1 Absorption Difference Spectroscopy of P700.- 3.1.2 Absorption Difference Spectroscopy of P680.- 3.1.3 Circular and Linear Dichroism of Photosystems 1 and 2.- 3.2 ESR and ENDOR.- 3.2.1 P700+.- 3.2.2 P680+.- 3.3 The Intermediary Acceptors of Photosystems 1 and 2.- 3.3.1 Photosystem 1.- 3.3.2 Photosystem 2.- 3.3.3 Triplet States.- 4 Structure of the Bacterial Primary Donor-Acceptor Complex.- 4.1 Electron Transfer Rates.- 4.2 Configuration of Primary Reactants.- References.- Notes Added in Proof (In Connection with Chapter 8).- 5: Triplet State and Chlorophylls.- Abbreviations.- 1 Introduction.- 2 Optical-Magnetic Resonance Spectroscopy.- 2.1 Triplet Detection. Zero Field Experiments.- 2.2 The Triplet State and the EPR Experiment.- 2.3 The Triplet Yield vs Magnetic Field.- 2.4 Triplet Photochemistry. The CIDEP Method.- 2.4.1 What is CIDEP?.- 2.4.2 Triplet Precursor vs Triplet Mechanism.- 2.4.3 The Triplet Mechanism.- 2.4.4 The Radical Pair Mechanism: ST+-1 Mixing.- 2.4.5 The Radical Pair Mechanism: ST0 Mixing.- 3 Triplet State Studies of Model Chlorophyll Compounds.- 4 In-Vivo Chlorophyll Triplets.- 4.1 Introduction.- 4.2 Bacterial Photosynthesis.- 4.2.1 The Triplet State in Bacterial Photosynthesis.- 4.2.2 Zero Field Splitting Parameters.- 4.2.3 Electron Spin Polarization in Triplets.- 4.3 Green Plant Photosynthesis.- 4.3.1 Photoexcited Triplet State Detection in Green Plants.- 4.3.2 CIDEP Studies of Photosynthesis.- 5 Summary.- References and Notes.- 6: The Chlorophyll Triplet State and the Structure of Chlorophyll Aggregates.- 1 Introduction.- 2 Optically Detected Magnetic Resonance in the Triplet State.- 3 Application of ODMR to the Chlorophyll Triplet State.- 3.1 Chlorophyll Triplet State Zero-Field Splittings.- 3.2 Chlorophyll T1 ? S0 Intersystem Crossing Rates.- 4 Application of Triplet State ODMR to Chlorophyll Aggregate Structure.- 4.1 The Triplet Exciton Model.- 4.2 Application to the Chlorophyll Dimer In Vitro.- 4.3 Chlorophyll Aggregate Structure In Vivo.- References.- 7: Synthetic Approaches to Photoreaction Center Structure and Function.- 1 Introduction.- 2 Porphyrin Models of Photoreaction Center Chlorophylls.- 3 Noncovalent Chlorophyll Special Pair Models.- 4 Preparation of Singly Linked Covalent Chlorophyll Dimers.- 5 Solvent-dependent Structure of Singly Linked Covalent Chlorophyll Dimers.- 6 Photophysical Properties of Singly Linked Covalent Chlorophyll Dimers.- 7 Photochemical Properties of Singly Linked Covalent Chlorophyll Dimers.- 8 Biomimetic Charge Separation Photochemistry.- 9 Doubly Linked Chlorophyll Cyclophane Models of Special Pair Structure.- 10 Concluding Remarks.- References.- 8: Light Path of Carbon Reduction in Photosynthesis.- 1 Introduction.- 2 Scope.- 2.1 Origin of O2 Evolution.- 2.2 Light and Dark Paths of Carbon.- 2.3 Submolecular Interactions of Chl-a Light Reactions.- 3 Model for Chlorophyll Light Reactions in Photosynthesis.- 3.1 Long-Wavelength Shifts of Chlorophyll Aggregates.- 3.2 Postulates.- 3.3 Path of Electrons from Water.- 4 Dimer Model of P700.- 4.1 Chlorophyll Purification.- 4.2 Mg... O(H)H Interactions.- 4.3 Model P700 Structure and Properties.- 5 P680 Model and Water Splitting.- 6 Carbon Reduction by Water.- 7 Two-Photon Activation of Water Splitting.- 8 Primary and Secondary Processes of Photosynthesis.- 8.1 Comparison of Models for P680 and P700.- 8.2 Light Reaction Sequence.- 8.3 Photochemical Reduction of CO2.- 8.4 Time Sequence and Branching of Electron Flow from Water..- 9 Further Conclusions.- 9.1 Spatial Relationships of P680 and P700.- 9.2 Quantum Requirement of Oxygen Evolution.- 9.3 PGA Reduction as Mechanism for Photoregulation.- References.- Notes Added in Proof for Chapter 4.- Author Index.

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詳細情報

  • NII書誌ID(NCID)
    BA03946396
  • ISBN
    • 3540113797
    • 0387113797
  • LCCN
    82005526
  • 出版国コード
    gw
  • タイトル言語コード
    eng
  • 本文言語コード
    eng
  • 出版地
    Berlin ; New York
  • ページ数/冊数
    xi, 342 p.
  • 大きさ
    25 cm
  • 分類
  • 件名
  • 親書誌ID
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