This textbook presents a concise comparison of catalytic and biocatalytic systems outlining their catalytic properties and peculiarities. Moreover, it presents a brief introduction to the science of catalysis and attempts to unify different catalytic systems into a single, conceptually coherent structure. In fact, molecular dynamics and complexity may occur in both catalysts and biocatalysts, with many similarities in both their structural configuration and operational mechanisms. Moreover, the interactions between the different components of the catalytic system that are important in defining the overall activity, including the nature of active sites are discussed. Each chapter includes end of chapter questions supported by an online instructor solution manual. This textbook will be useful for undergraduate and graduate chemistry and biochemistry students.
Author(s): Marco Piumetti
Publisher: Springer
Year: 2021
Language: English
Pages: 161
City: Cham
Preface
About This Book
Introduction
References
Contents
About the Author
1 Structure of Proteins
1.1 Introduction
1.2 Primary Structure
1.3 Secondary Structure
1.4 Tertiary Structure
1.5 Quaternary Structure
1.6 Driving Forces in Protein Folding
1.7 Structural Flexibility in Proteins
1.8 Thermodynamics of Protein–ligand Complexes
1.9 Characterization of Protein Structures [16]
1.9.1 X-Ray Crystallography
1.9.2 Nuclear Magnetic Resonance Spectroscopy
1.9.3 Cryo-Electron Microscopy
1.10 Summary
1.11 Questions
References
2 Enzymes and Their Function
2.1 Introduction
2.2 Structure of Enzymes
2.3 Enzymatic Process
2.4 Enzyme Kinetics
2.4.1 Single-Substrate Reactions
2.4.1.1 Michaelis–Menten Kinetics
2.4.2 Multisubstrate Reactions
2.4.3 Non-Michaelis–Menten Kinetics
2.5 Factors Influencing Enzyme Activity
2.5.1 Environmental Conditions: Temperature and pH
2.5.2 Activators and Inhibitors
2.5.2.1 Reversible Inhibition
2.5.2.2 Irreversible Inhibition
2.5.2.3 Allosteric Activation and Inhibition
2.6 Summary
2.7 Questions
References
3 Introduction to Molecular Catalysis
3.1 Science of Catalysis [1–3]
3.1.1 Homogeneous, Heterogeneous and Enzymatic Catalysis
3.1.2 Catalytic Activity, Selectivity and Yield
3.2 Kinetics of Catalytic Reactions [1, 6–8]
3.2.1 Reaction Rates
3.2.2 Transition State Theory [9]
3.2.3 The Arrhenius Equation
3.3 Fundamental Concepts in Heterogeneous Catalysis [5, 9–11]
3.3.1 Steps in Heterogeneous Catalysis
3.3.2 The Sabatier Principle
3.4 Chemisorption and Physisorption
3.4.1 Langmuir–Hinshelwood Versus Eley–Rideal Mechanism [11]
3.4.2 Mars and Van Krevelen Mechanism [11, 13, 14]
3.4.3 Deactivation of Catalytic Action [3]
3.5 Summary
3.6 Questions
References
4 Complex Nature of Active Sites
4.1 Dynamic Behaviour of Active Sites [1, 2]
4.2 Active Sites in Heterogeneous Catalysis: Historical Background [1, 2]
4.2.1 Single-Site Heterogeneous Catalysts [1, 2]
4.2.2 Small Metal Particles [1, 2]
4.2.3 Zeolites [2]
4.2.4 Oxide Catalysts [2]
4.3 Active Sites in Enzymatic Catalysis
4.3.1 Allosterically Regulated Enzymes: The Case of ATCase
4.3.2 Active Sites and Electric Fields
4.4 Active Sites in Homogenous Catalysis
4.4.1 Catalytic Cycles and Flexibility
4.5 Summary
4.6 Questions
References
5 Complexity in Catalysis
5.1 Self-organizing Systems [1]
5.2 Complexity of Catalytic Processes [9, 10]
5.2.1 Thermodynamic Considerations [9]
5.2.2 Topological Aspects of Catalytic Systems and Real Surfaces
5.3 Well- and Ill-Conditioned Systems [9]
5.4 Cooperation and Synergy
5.5 New Modelling Approaches for Decoding Complexity in Catalysis
5.5.1 The Theory of Hyperstructures
5.5.1.1 Cooperation and Synergetic Hyperstructures [16]
5.5.1.2 Strategic Relevance [16]
5.5.2 Application of Game Theory to Catalytic Systems [16]
5.6 Artificial Intelligence Faces Catalytic Complexity
5.7 Summary
5.8 Questions
References
