Stephen E. J. Rigby
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View article: A Noncanonical Tryptophan Analogue Reveals an Active Site Hydrogen Bond Controlling Ferryl Reactivity in a Heme Peroxidase
A Noncanonical Tryptophan Analogue Reveals an Active Site Hydrogen Bond Controlling Ferryl Reactivity in a Heme Peroxidase Open
Nature employs high-energy metal-oxo intermediates embedded within enzyme active sites to perform challenging oxidative transformations with remarkable selectivity. Understanding how different local metal-oxo coordination environments cont…
View article: Structure and Mechanism of <i>Pseudomonas aeruginosa</i> PA0254/HudA, a prFMN-Dependent Pyrrole-2-carboxylic Acid Decarboxylase Linked to Virulence
Structure and Mechanism of <i>Pseudomonas aeruginosa</i> PA0254/HudA, a prFMN-Dependent Pyrrole-2-carboxylic Acid Decarboxylase Linked to Virulence Open
The UbiD family of reversible (de)carboxylases depends on the recently discovered prenylated-FMN (prFMN) cofactor for activity. The model enzyme ferulic acid decarboxylase (Fdc1) decarboxylates unsaturated aliphatic acids via a reversible …
View article: Issue Information
Issue Information Open
Aim and ScopeInfluenza and other respiratory viruses is the Official Journal of the International Society of Influenza and other respiratory virus diseases -an independent scientific professional society -dedicated to promoting the prevent…
View article: Catabolic Reductive Dehalogenase Substrate Complex Structures Underpin Rational Repurposing of Substrate Scope
Catabolic Reductive Dehalogenase Substrate Complex Structures Underpin Rational Repurposing of Substrate Scope Open
Reductive dehalogenases are responsible for the reductive cleavage of carbon-halogen bonds during organohalide respiration. A variety of mechanisms have been proposed for these cobalamin and [4Fe-4S] containing enzymes, including organocob…
View article: Rewiring the “Push-Pull” Catalytic Machinery of a Heme Enzyme Using an Expanded Genetic Code
Rewiring the “Push-Pull” Catalytic Machinery of a Heme Enzyme Using an Expanded Genetic Code Open
Nature employs a limited number of genetically encoded axial ligands to control diverse heme enzyme activities. Deciphering the functional significance of these ligands requires a quantitative understanding of how their electron-donating c…
View article: Regioselective <i>para</i>‐Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase
Regioselective <i>para</i>‐Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase Open
The utilization of CO 2 as a carbon source for organic synthesis meets the urgent demand for more sustainability in the production of chemicals. Herein, we report on the enzyme‐catalyzed para ‐carboxylation of catechols, employing 3,4‐dihy…
View article: Expression, Purification, and Biochemical Characterization of the Flavocytochrome P450 CYP505A30 from <i>Myceliophthora thermophila</i>
Expression, Purification, and Biochemical Characterization of the Flavocytochrome P450 CYP505A30 from <i>Myceliophthora thermophila</i> Open
The cytochrome P450/P450 reductase fusion enzyme CYP505A30 from the thermophilic fungus Myceliophthora thermophila and its heme (P450) domain were expressed in Escherichia coli and purified using affinity, ion exchange, and size exclusion …
View article: Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis
Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis Open
The activity of the reversible decarboxylase enzyme Fdc1 is dependent on prenylated FMN (prFMN), a recently discovered cofactor. The oxidized prFMN supports a 1,3-dipolar cycloaddition mechanism that underpins reversible decarboxylation. F…
View article: Catalytic Determinants of Alkene Production by the Cytochrome P450 Peroxygenase OleTJE
Catalytic Determinants of Alkene Production by the Cytochrome P450 Peroxygenase OleTJE Open
The Jeotgalicoccus sp. peroxygenase cytochrome P450 OleTJE (CYP152L1) is a hydrogen peroxide-driven oxidase that catalyzes oxidative decarboxylation of fatty acids, producing terminal alkenes with applications as fine chemicals and biofuel…
View article: Analysis of Heme Iron Coordination in DGCR8: The Heme-Binding Component of the Microprocessor Complex
Analysis of Heme Iron Coordination in DGCR8: The Heme-Binding Component of the Microprocessor Complex Open
DGCR8 is the RNA-binding partner of the nuclease Drosha. Their complex (the "Microprocessor") is essential for processing of long, primary microRNAs (pri-miRNAs) in the nucleus. Binding of heme to DGCR8 is essential for pri-miRNA processin…