Artificial Metalloproteins

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