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Mononuclear Non-heme Iron Dependent Enzymes
- 1st Edition, Volume 703 - September 1, 2024
- Editors: Anna Maria Pyle, Jennifer Bridwell-Rabb, David Christianson
- Language: English
- Hardback ISBN:9 7 8 - 0 - 4 4 3 - 3 1 3 0 4 - 2
- eBook ISBN:9 7 8 - 0 - 4 4 3 - 3 1 3 0 5 - 9
Mononuclear Non-heme Iron Dependent Enzymes, Volume 703 focuses on methods for studying, characterizing, and leveraging the chemistry of mononuclear non-heme iron dependent enzyme… Read more
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Request a sales quoteMononuclear Non-heme Iron Dependent Enzymes, Volume 703 focuses on methods for studying, characterizing, and leveraging the chemistry of mononuclear non-heme iron dependent enzymes. Chapters in this new release include Photoreduction for Rieske oxygenase chemistry, Insights into the Mechanisms of Rieske Oxygenases from Studying the Unproductive Activation of Dioxygen, Non-heme iron and 2-oxoglutarate enzymes catalyze cyclopropane and azacyclopropane formations, Obtaining precise metrics of substrate positioning in Fe(II)/2OG dependent enzymes using Hyperfine Sublevel Correlation Spectroscopy, Xe-pressurization studies for revealing substrate-entrance tunnels, and much more.
Additional chapters cover A tale of two dehydrogenases involved in NADH recycling, Rieske oxygenases and/or their partner reductase proteins, Expression, assay and inhibition of 9-cis-epoxycarotenoid dioxygenase (NCED) from Solanum lycopersicum and Zea mays, Biocatalysis and non-heme iron enzymes, In vitro analysis of the three-component Rieske oxygenase cumene dioxygenase from Pseudomonas fluorescens IP01, Structure and function of carbazole 1,9a-dioxygenase, Characterization of a Mononuclear Nonheme Iron-dependent Mono-oxygenase OzmD in Oxazinomycin Biosynthesis, and much more.
Additional chapters cover A tale of two dehydrogenases involved in NADH recycling, Rieske oxygenases and/or their partner reductase proteins, Expression, assay and inhibition of 9-cis-epoxycarotenoid dioxygenase (NCED) from Solanum lycopersicum and Zea mays, Biocatalysis and non-heme iron enzymes, In vitro analysis of the three-component Rieske oxygenase cumene dioxygenase from Pseudomonas fluorescens IP01, Structure and function of carbazole 1,9a-dioxygenase, Characterization of a Mononuclear Nonheme Iron-dependent Mono-oxygenase OzmD in Oxazinomycin Biosynthesis, and much more.
- Provides detailed articles regarding how to study the structures and mechanisms of mononuclear non-heme iron dependent enzymes
- Guides readers on how to use partner proteins in non-heme iron enzyme catalysis
- Includes strategies to employ mononuclear non-heme iron enzymes in biocatalytic applications
Chemists who study the remarkable transformations that are facilitated by metalloproteins. Scientists who are interested in purifying, crystallizing, mechanistically studying the chemistry of mononuclear non-heme iron enzymes, and/or leveraging the chemistry of these enzymes for biocatalytic endeavors
- Cover image
- Title page
- Table of Contents
- Series Page
- Copyright
- Contributors
- Section 1: Methods for studying the catalytic mechanisms of mononuclear non-heme iron dependent enzymes
- Chapter One: Characterization of O2 uncoupling in biodegradation reactions of nitroaromatic contaminants catalyzed by rieske oxygenases
- Abstract
- 1 Introduction
- 2 Mass Balances and Reaction Stoichiometries
- 3 Quantification of transient reactive oxygen species
- 4 Reaction kinetics
- 5 Summary and Conclusions
- Acknowledgments
- References
- Chapter Two: Spectroscopic definition of ferrous active sites in non-heme iron enzymes
- Abstract
- 1 d6 Ligand field theory (LFT)
- 2 LF spectroscopy = low temperature magnetic circular dichroism (LT MCD)
- 3 Variable-temperature, variable-field (VTVH) MCD
- 4 LFT of spin-hamiltonian parameters from VTVH MCD
- 5 An early application of VTVH MCD on a non-heme Fe(II) enzyme
- 6 Perspective
- Acknowledgments
- References
- Chapter Three: Equilibrium dialysis with HPLC detection to measure substrate binding affinity of a non-heme iron halogenase
- Abstract
- 1 Introduction
- 2 Materials
- 3 Methods
- 4 Conclusions
- References
- Chapter Four: Preparation of reductases for multicomponent oxygenases
- Abstract
- 1 Introduction
- 2 General safety
- 3 Reductase production and activity
- 4 Codon optimization and protein purification
- 5 Protein characterization
- 6 Summary and conclusions
- References
- Chapter Five: Development of a rapid mass spectrometric method for the analysis of ten-eleven translocation enzymes
- Abstract
- 1 Introduction
- 2 Preparation of the materials
- 3 Biochemical assays and results
- 4 Notes
- Funding
- References
- Chapter Six: Non-standard amino acid incorporation into thiol dioxygenases
- Abstract
- 1 Overview
- 2 Eukaryotic thiol dioxygenases
- 3 Genetic code expansion
- 4 Application to thiol dioxygenases
- 5 Conclusions
- Acknowledgments
- References
- Further reading
- Chapter Seven: Unveiling the mechanism of cysteamine dioxygenase: A combined HPLC-MS assay and metal-substitution approach
- Abstract
- 1 Introduction
- 2 Protein expression, purification, and crystallization
- 3 Spectral characterization of Co-ADO
- 4 Cobalt reconstitution in ADO
- 5 HPLC-MS analysis of the hypotaurine formation by ADO
- 6 Summary and conclusions
- Acknowledgments
- References
- Chapter Eight: In vitro analysis of the three-component Rieske oxygenase cumene dioxygenase from Pseudomonas fluorescens IP01
- Abstract
- 1 Introduction
- 2 In vitro analysis of Rieske oxygenases
- 3 Expression of Cumene dioxygenase
- 4 Step-by-step method details
- 5 General considerations
- 6 Cell lysis and protein purification
- 7 Step-by-step method details
- 8 General considerations
- 9 Enzymatic activity assay
- 10 Step-by-step method details
- 11 General considerations
- 12 Summary and conclusions
- Acknowledgments
- References
- Section 2: Leveraging mononuclear non-heme iron enzymes for biocatalysis
- Chapter Nine: Radical-relay C(sp3)–H azidation catalyzed by an engineered nonheme iron enzyme
- Abstract
- 1 Introduction
- 2 Materials
- 3 Protocols
- 4 Summary
- Acknowledgments
- References
- Chapter Ten: Purification and characterization of a Rieske oxygenase and its NADH-regenerating partner proteins
- Abstract
- 1 Introduction
- 2 Considerations for assembling a Rieske oxygenase pathway in vitro
- 3 Protein constructs for recombinant expression and purification
- 4 Recombinant expression and purification of the TsaM, TsaC, TsaD, and VanB
- 5 Methods for assessing the quality of the purified TsaMBCD pathway proteins
- 6 Enzymatic assays for the TsaMBCD pathway
- 7 Crystallization of the short-chain dehydrogenase/reductase (SDR) enzyme TsaC
- 8 Conclusions
- Acknowledgments
- References
- Chapter Eleven: Whole-cell Rieske non-heme iron biocatalysts
- Abstract
- 1 Introduction
- 2 Before you begin timing: 4–5 days
- 3 Key resources table
- 4 Materials and equipment
- 5 Step-by-step method details
- 6 High-performance liquid chromatography (HPLC) analysis
- 7 Establishing a calibration curve
- 8 Expected outcomes
- 9 Quantification and statistical analysis
- 10 Advantages
- 11 Limitations
- 12 Optimization and troubleshooting
- 13 Safety considerations and standards
- 14 Alternative methods/procedures
- References
- Chapter Twelve: Photo-reduction facilitated stachydrine oxidative N-demethylation reaction: A case study of Rieske non-heme iron oxygenase Stc2 from Sinorhizobium meliloti
- Abstract
- Abbreviations
- 1 Introduction
- 2 Heterologous expression and purification of Stc2
- 3 Materials and equipment
- 4 Step-by-step procedure details
- 5 Expected outcomes, advantages, and disadvantages
- 6 Optimization and troubleshooting
- 7 Safety considerations and standards
- 8 Stc2 characterization
- 9 Materials and equipment
- 10 Step-by-step details
- 11 Stc2 photo-reduction using eosin Y and Na2SO3
- 12 Materials and equipment
- 13 Step-by-step method details
- References
- Chapter Thirteen: Functional and spectroscopic approaches to determining thermal limitations of Rieske oxygenases
- Abstract
- 1 Introduction
- 2 Expression and purification of a RO system
- 3 Iron cofactor lability
- 4 Temperature dependent kinetics
- 5 Lifetime
- 6 Differential scanning calorimetry (DSC)
- References
- No. of pages: 412
- Language: English
- Edition: 1
- Volume: 703
- Published: September 1, 2024
- Imprint: Academic Press
- Hardback ISBN: 9780443313042
- eBook ISBN: 9780443313059
DC
David Christianson
After completing studies for the A.B., A.M., and Ph.D. degrees in chemistry at Harvard University, David W. Christianson joined the faculty of the University of Pennsylvania, where he is currently the Roy and Diana Vagelos Professor in Chemistry and Chemical Biology. At Penn, Christianson’s research focuses on the structural and chemical biology of the zinc-dependent histone deacetylases as well as enzymes of terpene biosynthesis. His research accomplishments have been recognized by several awards, including the Pfizer Award in Enzyme Chemistry and the Repligen Award in Chemistry of Biological Processes from the American Chemical Society, a Guggenheim Fellowship, and the Elizabeth S. and Richard M. Cashin Fellowship from the Radcliffe Institute for Advanced Study at Harvard University. Christianson is also a dedicated classroom teacher, and his accomplishments in this regard have been recognized by the Lindback Award for Distinguished Teaching at Penn and a Rhodes Trust Inspirational Educator Award from Oxford University. Christianson has also held visiting professorships in the Department of Biochemistry at Cambridge University and the Department of Chemistry and Chemical Biology at Harvard University. Christianson has served with Prof. Anna Pyle as Co-Editor-in-Chief of Methods in Enzymology since 2015.
Affiliations and expertise
University of Pennsylvania, USARead Mononuclear Non-heme Iron Dependent Enzymes on ScienceDirect