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Artificial Metalloproteins covers artificial metalloproteins (ArMs) and how they have emerged as powerful vehicles with which to control, implement, and leverage the unique reactivity and spectroscopic properties of their bound metal ions. Chapters in this release include Incorporating Non-Native Cofactors into Heme Proteins, Designing 4-Helix Bundles to Bind Porphyrin/Porphyrin-like Cofactors, Cobalt-Substituted Hemoprotein Expression, Rationally designed directed evolution of cytochrome P450 enzymes, De novo design of a switchable a-helical hemoprotein, Primary Coordination Sphere Part B: Unnatural Metal-Binding Sites Beyond the Heme, and more.

Other sections cover Unnatural Amino Acid Incorporation for Creating Artificial Metalloenzymes, Development of a PQQ-Dependent Artificial Metalloprotein, Evolutionary Engineering of a Rhodium Complex-Linked Artificial Metalloenzyme, Design and Application of Nonheme Iron Enzymes, Part C: Secondary Sphere Modulation for Metallocofactor Activation, Designing Artificial Metalloenzymes by Engineering the Primary and Secondary Coordination Sphere in Native Protein Scaffolds, and much more.

  • Presents a wide variety of strategies for the installation of nonnative metal binding sites
  • Includes protein engineering approaches ranging from modulating secondary coordination sphere effects around the metal ion to the implementation of peptide dynamical motions for the regulation of these effects
  • Provides a ‘how-to’ guide for the interdisciplinary techniques needed in the construction and characterization of diverse ArM systems

1. Title of Book - p. i 2. Cover image - p. i 3. Title page - p. ii 4. Table of Contents - p. iii 5. Series Page - p. iii 6. Copyright - p. iv 7. Contributors - p. xv 8. Preface - p. xix 9. Chapter One: De novo design of four-helix bundle proteins to bind metalloporphyrin cofactors - p. 1 10. Chapter Two: The direct expression of apo heme proteins: A general strategy to obtain designer heme proteins with abiological cofactors - p. 23 11. Chapter Three: Cobalt-substituted hemoprotein expression - p. 55 12. Chapter Four: Design and preparation of artificial heme-copper enzymes - p. 77 13. Chapter Five: De Novo design of α-helical heme binding proteins capable of versatile cofactor ligation - p. 115 14. Chapter Six: A bipyridyl noncanonical amino acid for expanding the scope of metalloprotein design - p. 141 15. Chapter Seven: Engineering an artificial metalloenzyme with a quinone coenzyme - p. 189 16. Chapter Eight: Reprogramming nonheme iron enzymes for abiotic alkene trifluoromethylazidation - p. 219 17. Chapter Nine: Computational tools in rational metalloenzyme design - p. 239 18. Chapter Ten: Chemical methods to stabilize segments of metalloproteins in the form of peptides - p. 265 19. Chapter Eleven: Breaking symmetry: Metal-guided assembly of heterotrimeric coiled coils - p. 293 20. Chapter Twelve: Design, engineering, and characterization of switchable artificial metalloproteins (swArMs) - p. 313 21. Chapter Thirteen: Tuning the function of de novo designed artificial Cu proteins by modulating reorganization energies - p. 349 22. Chapter Fourteen: Evaluation of biocatalysts for artificial photosynthesis - p. 377

Descripcion
Descripción

Artificial Metalloproteins covers artificial metalloproteins (ArMs) and how they have emerged as powerful vehicles with which to control, implement, and leverage the unique reactivity and spectroscopic properties of their bound metal ions. Chapters in this release include Incorporating Non-Native Cofactors into Heme Proteins, Designing 4-Helix Bundles to Bind Porphyrin/Porphyrin-like Cofactors, Cobalt-Substituted Hemoprotein Expression, Rationally designed directed evolution of cytochrome P450 enzymes, De novo design of a switchable a-helical hemoprotein, Primary Coordination Sphere Part B: Unnatural Metal-Binding Sites Beyond the Heme, and more.

Other sections cover Unnatural Amino Acid Incorporation for Creating Artificial Metalloenzymes, Development of a PQQ-Dependent Artificial Metalloprotein, Evolutionary Engineering of a Rhodium Complex-Linked Artificial Metalloenzyme, Design and Application of Nonheme Iron Enzymes, Part C: Secondary Sphere Modulation for Metallocofactor Activation, Designing Artificial Metalloenzymes by Engineering the Primary and Secondary Coordination Sphere in Native Protein Scaffolds, and much more.

  • Presents a wide variety of strategies for the installation of nonnative metal binding sites
  • Includes protein engineering approaches ranging from modulating secondary coordination sphere effects around the metal ion to the implementation of peptide dynamical motions for the regulation of these effects
  • Provides a ‘how-to’ guide for the interdisciplinary techniques needed in the construction and characterization of diverse ArM systems

1. Title of Book - p. i 2. Cover image - p. i 3. Title page - p. ii 4. Table of Contents - p. iii 5. Series Page - p. iii 6. Copyright - p. iv 7. Contributors - p. xv 8. Preface - p. xix 9. Chapter One: De novo design of four-helix bundle proteins to bind metalloporphyrin cofactors - p. 1 10. Chapter Two: The direct expression of apo heme proteins: A general strategy to obtain designer heme proteins with abiological cofactors - p. 23 11. Chapter Three: Cobalt-substituted hemoprotein expression - p. 55 12. Chapter Four: Design and preparation of artificial heme-copper enzymes - p. 77 13. Chapter Five: De Novo design of α-helical heme binding proteins capable of versatile cofactor ligation - p. 115 14. Chapter Six: A bipyridyl noncanonical amino acid for expanding the scope of metalloprotein design - p. 141 15. Chapter Seven: Engineering an artificial metalloenzyme with a quinone coenzyme - p. 189 16. Chapter Eight: Reprogramming nonheme iron enzymes for abiotic alkene trifluoromethylazidation - p. 219 17. Chapter Nine: Computational tools in rational metalloenzyme design - p. 239 18. Chapter Ten: Chemical methods to stabilize segments of metalloproteins in the form of peptides - p. 265 19. Chapter Eleven: Breaking symmetry: Metal-guided assembly of heterotrimeric coiled coils - p. 293 20. Chapter Twelve: Design, engineering, and characterization of switchable artificial metalloproteins (swArMs) - p. 313 21. Chapter Thirteen: Tuning the function of de novo designed artificial Cu proteins by modulating reorganization energies - p. 349 22. Chapter Fourteen: Evaluation of biocatalysts for artificial photosynthesis - p. 377

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