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Time-resolved scattering methods for biological samples at the CoSAXS beamline, MAX IV Laboratory.
Methods Enzymol
November 2024
MAX IV Laboratory, Lund University, Lund, Sweden. Electronic address:
Article Synopsis
- - CoSAXS is a cutting-edge SAXS/WAXS beamline at the MAX IV synchrotron, designed for high brilliance and capable of millisecond time-resolved scattering to study protein dynamics in solution.
- - It incorporates innovative sample environments such as UV-vis and fluorescence spectroscopy for in-depth analysis of protein conformational changes during acid-driven denaturation, as well as microfluidic chips for efficient sample volume usage.
- - The setup allows for precise studies of protein behaviors under various conditions, utilizing techniques like stopped-flow SAXS and laser "pumping" to observe rapid structural changes at low q values, showcasing its stability and low background interference.
Temperature-Driven Stopped-Flow Experiments for Investigating the Initial Aggregation of the α-Synuclein Amyloid Protein, Focusing on Active and Inactive Phases.
J Fluoresc
October 2024
Centro de Química Estrutural, Institute of Molecular Sciences, Instituto Superior Técnico, University of Lisbon, Campus Alameda, Av. Rovisco Pais, Lisbon, 1049-001, Portugal.
The primary objective of this research is to further examine the events occurring during the active or burst phase by focusing on the aggregation of the Syn amyloid protein. Regarding this aspect, it was initially conducted rapid temperature variations using stopped-flow spectrometry and tyrosyl group fluorescence emission detection, within the initial 500 milliseconds in buffered Syn solutions at pH 7, exploring various temperature ranges to investigate protein aggregation. The results obtained were contrasted with results obtained for the N-acetyl-L-tyrosinamide (NAYA) parent compound in the same conditions.
View Article and Find Full Text PDFExpanding the Clip-and-Cleave Concept: Approaching Enantioselective C-H Hydroxylations by Copper Imine Complexes Using O and HO as Oxidants.
J Am Chem Soc
September 2024
Institute of Inorganic and Analytical Chemistry, Justus Liebig University Giessen, 35392 Giessen, Germany.
Copper-mediated aromatic and aliphatic C-H hydroxylations using benign oxidants (O and HO) have been studied intensively in recent years to meet the growing demand for efficient and green C-H functionalizations. Herein, we report an enantioselective variant of the so-called clip-and-cleave concept for intramolecular ligand hydroxylations by the application of chiral diamines as directing groups. We tested the hydroxylation of cyclohexanone and 1-acetyladamantane under different oxidative conditions (Cu/O; Cu/HO; Cu/HO) in various solvents.
View Article and Find Full Text PDFExploring the influence of H-bonding and ligand constraints on thiolate ligated non-heme iron mediated dioxygen activation.
Chem Sci
August 2024
Department of Chemistry, University of Washington Campus Box 351700 Seattle WA 98195 USA
Converting triplet dioxygen into a powerful oxidant is fundamentally important to life. The study reported herein quantitatively examines the formation of a well-characterized, reactive, O-derived thiolate ligated Fe-superoxo using low-temperature stopped-flow kinetics. Comparison of the kinetic barriers to the formation of this species two routes, involving either the addition of (a) O to [Fe(S N(Pr,Pr))] (1) or (b) superoxide to [Fe(S N(Pr,Pr))] (3) is shown to provide insight into the mechanism of O activation.
View Article and Find Full Text PDFVibrational analyses of the reaction of oxymyoglobin with NO using a photolabile caged NO donor at cryogenic temperatures.
J Inorg Biochem
September 2024
Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA. Electronic address:
The NO dioxygenation reaction catalyzed by heme-containing globin proteins is a crucial aerobic detoxification pathway. Accordingly, the second order reaction of NO with oxymyoglobin and oxyhemoglobin has been the focus of a large number of kinetic and spectroscopic studies. Stopped-flow and rapid-freeze-quench (RFQ) measurements have provided evidence for the formation of a Fe(III)-nitrato complex with millisecond lifetime prior to release of the nitrate product, but the temporal resolution of these techniques is insufficient for the characterization of precursor species.
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