Results 41 to 50 of about 2,176,446 (301)

Reconstructing enzyme evolution by protein engineering

open access: yesFEBS Letters, EarlyView.
Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler   +2 more
wiley   +1 more source

Coordinating ability and versatility of organosulfur-based ligands in transition metal catalyzed hydrogenative and hydrogen auto-transfer processes

open access: yesFrontiers in Chemistry
Transition metal complexes with sulfur-donor ligands serve as efficient catalysts in numerous homogeneous reactions, owing to the coordination diversity of sulfur-based ligands and the possibility to obtain chiral and achiral complexes.
Andrei Paraschiv   +5 more
doaj   +1 more source

Poisoning effect of N-containing compounds on performance of Raney® nickel in transfer hydrogenation

open access: yesCatalysis Communications, 2021
The effect of amines, imines and heterocycle compounds on conversion has been studied in transfer hydrogenation of camphor and 2-PrOH catalyzed by Raney® nickel.
Alexey A. Philippov, Oleg N. Martyanov
doaj   +1 more source

Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation

open access: yesFEBS Letters, EarlyView.
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang   +2 more
wiley   +1 more source

Emerging experimental and computational methods for studying redox‐regulated structural transitions

open access: yesFEBS Letters, EarlyView.
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass   +2 more
wiley   +1 more source

TiO2 Photocatalysis for Transfer Hydrogenation

open access: yesMolecules, 2019
Catalytic transfer hydrogenation reactions, based on hydrogen sources other than gaseous H2, are important processes that are preferential in both laboratories and factories.
Dongge Ma   +4 more
doaj   +1 more source

Iridium-catalyzed asymmetric transfer hydrogenation of quinolines with Hantzsch esters

open access: yes, 2007
The iridium-catalyzed enantioselective transfer hydrogenation of quinolines with Hantzsch esters was developed with up to 88%, ee using [Ir(COD)Cl](2)/(S)-SegPhos/I-2 as a catalyst.
Zeng, Wei   +3 more
core   +1 more source

Structural and biochemical analysis of a B12 superbinder

open access: yesFEBS Letters, EarlyView.
BtuG proteins are vitamin B12 scavengers in Bacteroides thetaiotaomicron, a dominant human gut bacterium. We present crystal structures of three BtuG homologs bound to cobalamin and its precursor cobinamide, revealing picomolar binding affinities, among the highest known for any natural protein.
Jose M. Martinez Felices   +3 more
wiley   +1 more source

Synthesis, structural characterization and biological activities of metal(II) complexes with Schiff bases derived from 5-bromosalicylaldehyde: Ru(II) complexes transfer hydrogenation

open access: yesJournal of Saudi Chemical Society, 2019
In this study, two novel Schiff base ligands (L1 and L2) derived from condensation of methyl 2-amino-6-methyl-4,5,6,7-tetrahydrothieno[2,3-c]pyridine-3-carboxylate and methyl 2-amino-6-phenyl-4,5,6,7-tetrahydrobenzo[b]thiophene-3-carboxylate, both ...
Kenan Buldurun   +3 more
doaj   +1 more source

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

open access: yesFEBS Letters, EarlyView.
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav   +2 more
wiley   +1 more source

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