Frederick Stull
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View article: Dehydrogenases in the Flavoprotein Amine Oxidoreductase Superfamily
Dehydrogenases in the Flavoprotein Amine Oxidoreductase Superfamily Open
Enzymes of the ubiquitous flavoprotein amine oxidoreductase (FAO) superfamily catalyze C-N bond oxidation of amine-containing substrates using flavin adenine dinucleotide (FAD) as a prosthetic group. Their reaction proceeds via a two-step …
View article: Role of glutamate 292 and lysine 331 in catalysis for the flavoenzyme (S)-6-hydroxynicotine oxidase from <i>Shinella</i> sp. HZN7
Role of glutamate 292 and lysine 331 in catalysis for the flavoenzyme (S)-6-hydroxynicotine oxidase from <i>Shinella</i> sp. HZN7 Open
The flavoenzyme NctB from Shinella sp. HZN7 catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine concomitant with dioxygen reduction, which is the same chemistry catalyzed by the well-studied flavoenzyme L-6-hydro…
View article: Ancestral evolution of oxidase activity in a class of (S)-nicotine and (S)-6-hydroxynicotine degrading flavoenzymes
Ancestral evolution of oxidase activity in a class of (S)-nicotine and (S)-6-hydroxynicotine degrading flavoenzymes Open
Reduced flavin cofactors have the innate ability to reduce molecular oxygen to hydrogen peroxide. Flavoprotein oxidases turbocharge the reaction of their flavin cofactor with oxygen whereas flavoprotein dehydrogenases generally suppress it…
View article: G-quadruplexes catalyze protein folding by reshaping the energetic landscape
G-quadruplexes catalyze protein folding by reshaping the energetic landscape Open
Many proteins have slow folding times in vitro that are physiologically untenable. To combat this challenge, ATP-dependent chaperonins are thought to possess the unique ability to catalyze protein folding. Performing quantitative model sel…
View article: G-quadruplexes catalyze protein folding by reshaping the energetic landscape
G-quadruplexes catalyze protein folding by reshaping the energetic landscape Open
proteins Many proteins have slow folding times in vitro that are physiologically untenable. To combat this challenge, ATP-dependent chaperonins are thought to possess the unique ability to catalyze protein folding. Performing quantitative …
View article: Rational design of a flavoenzyme for aerobic nicotine catabolism
Rational design of a flavoenzyme for aerobic nicotine catabolism Open
Enzymatic therapy with nicotine-degrading enzyme is a new strategy in treating nicotine addiction, which can reduce nicotine concentrations and weaken withdrawal in the rat model. However, when O 2 is used as the electron acceptor, no sati…
View article: Rational Design of a Flavoenzyme for Aerobic Nicotine Catabolism
Rational Design of a Flavoenzyme for Aerobic Nicotine Catabolism Open
Enzymatic therapy with nicotine-degrading enzyme is a new strategy in treating nicotine addiction, which can reduce nicotine concentrations and weaken withdrawal in the rat model. However, when O 2 is used as the electron acceptor, no sati…
View article: Breaking the habit: isolating nicotine-degrading bacteria in undergraduate microbiology teaching labs
Breaking the habit: isolating nicotine-degrading bacteria in undergraduate microbiology teaching labs Open
Nicotine is a major alkaloid in tobacco plants and an addictive component of tobacco products. Some bacteria grow on tobacco plants and have evolved the ability to metabolize nicotine. As part of our microbiology teaching lab, we used mini…
View article: Hypothiocyanous acid reductase is critical for host colonization and infection by Streptococcus pneumoniae
Hypothiocyanous acid reductase is critical for host colonization and infection by Streptococcus pneumoniae Open
The major human pathogen Streptococcus pneumoniae encounters the immune-derived oxidant hypothiocyanous acid (HOSCN) at sites of colonization and infection. We recently identified the pneumococcal hypothiocyanous acid reductase (Har), a me…
View article: Directed evolution unlocks oxygen reactivity for a nicotine-degrading flavoenzyme
Directed evolution unlocks oxygen reactivity for a nicotine-degrading flavoenzyme Open
The flavoenzyme nicotine oxidoreductase (NicA2) is a promising injectable treatment to aid in the cessation of smoking, a behavior responsible for one in ten deaths worldwide. NicA2 acts by degrading nicotine in the bloodstream before it r…
View article: Analysis of histidine‐tagged recombinant proteins from nickel and copper coated surfaces by direct electrospray ionization and desorption electrospray ionization mass spectrometry
Analysis of histidine‐tagged recombinant proteins from nickel and copper coated surfaces by direct electrospray ionization and desorption electrospray ionization mass spectrometry Open
Rationale Purification of recombinant proteins is a necessary step for functional or structural studies and other applications. Immobilized metal affinity chromatography is a common recombinant protein purification method. Mass spectrometr…
View article: Binding Interface and Electron Transfer Between Nicotine Oxidoreductase and Its Cytochrome c Electron Acceptor
Binding Interface and Electron Transfer Between Nicotine Oxidoreductase and Its Cytochrome c Electron Acceptor Open
The enzyme nicotine oxidoreductase (NicA2) is a member of the flavoprotein amine oxidase family that uses a cytochrome c protein (CycN) as its oxidant instead of dioxygen, which is the oxidant used by most other members of this enzyme fami…
View article: <i>Escherichia coli</i> RclA is a highly active hypothiocyanite reductase
<i>Escherichia coli</i> RclA is a highly active hypothiocyanite reductase Open
Hypothiocyanite and hypothiocyanous acid (OSCN − /HOSCN) are pseudohypohalous acids released by the innate immune system which are capable of rapidly oxidizing sulfur-containing amino acids, causing significant protein aggregation and dama…
View article: The enzyme pseudooxynicotine amine oxidase from Pseudomonas putida S16 is not an oxidase, but a dehydrogenase
The enzyme pseudooxynicotine amine oxidase from Pseudomonas putida S16 is not an oxidase, but a dehydrogenase Open
The soil-dwelling bacterium Pseudomonas putida S16 can survive on nicotine as its sole carbon and nitrogen source. The enzymes nicotine oxidoreductase (NicA2) and pseudooxynicotine amine oxidase (Pnao), both members of the flavin-containin…
View article: Bacterial flavoprotein monooxygenase YxeK salvages toxic <i>S</i>‐(2‐succino)‐adducts via oxygenolytic C–S bond cleavage
Bacterial flavoprotein monooxygenase YxeK salvages toxic <i>S</i>‐(2‐succino)‐adducts via oxygenolytic C–S bond cleavage Open
Thiol‐containing nucleophiles such as cysteine react spontaneously with the citric acid cycle intermediate fumarate to form S ‐(2‐succino)‐adducts. In Bacillus subtilis , a salvaging pathway encoded by the yxe operon has recently been iden…
View article: SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins
SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins Open
The assembly of small disordered proteins into highly ordered amyloid fibrils in Alzheimer’s and Parkinson’s patients is closely associated with dementia and neurodegeneration. Understanding the process of amyloid formation is thus crucial…
View article: Periplasmic Chaperones and Prolyl Isomerases
Periplasmic Chaperones and Prolyl Isomerases Open
The biogenesis of periplasmic and outer membrane proteins (OMPs) in Escherichia coli is assisted by a variety of processes that help with their folding and transport to their final destination in the cellular envelope. Chaperones are macro…
View article: Enzymatic control of dioxygen binding and functionalization of the flavin cofactor
Enzymatic control of dioxygen binding and functionalization of the flavin cofactor Open
Significance Vitamins are often precursors for the biosynthesis of organic enzyme cofactors, as exemplified by the ubiquitous vitamin B2-derived flavins. Enzymes employ flavins, e.g., to oxygenate organic substrates with the help of covale…
View article: Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase
Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase Open
Many microorganisms use flavin-dependent thymidylate synthase (FDTS) to synthesize the essential nucleotide 2'-deoxythymidine 5'-monophosphate (dTMP) from 2'-deoxyuridine 5'-monophosphate (dUMP), 5,10-methylenetetrahydrofolate (CH2THF), an…
View article: Biochemical Establishment and Characterization of EncM’s Flavin-N5-oxide Cofactor
Biochemical Establishment and Characterization of EncM’s Flavin-N5-oxide Cofactor Open
The ubiquitous flavin-dependent monooxygenases commonly catalyze oxygenation reactions by means of a transient C4a-peroxyflavin. A recent study, however, suggested an unprecedented flavin-oxygenating species, proposed as the flavin-N5-oxid…