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[BOK][B] Introduction to proteins: structure, function, and motion
Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …
structure, function, and motion of proteins for students, faculty, and researchers at all levels …
Relating localized protein motions to the reaction coordinate in coenzyme B12‐dependent enzymes
The classical picture of enzyme catalysis relies on controlling the entropic and enthalpic
contributions by manipulating reaction barriers and co‐locating reactants and cofactors to …
contributions by manipulating reaction barriers and co‐locating reactants and cofactors to …
Non-Aufbau electronic structure in radical enzymes and control of the highly reactive intermediates
MH Khalilian, GA DiLabio - Chemical Science, 2024 - pubs.rsc.org
Radicals are highly reactive, short-lived chemical species that normally react
indiscriminately with biological materials, and yet, nature has evolved thousands of enzymes …
indiscriminately with biological materials, and yet, nature has evolved thousands of enzymes …
Large-Scale Domain Motions and Pyridoxal-5'-Phosphate Assisted Radical Catalysis in Coenzyme B12-Dependent Aminomutases †
AN Maity, YH Chen, SC Ke - International Journal of Molecular Sciences, 2014 - mdpi.com
Lysine 5, 6-aminomutase (5, 6-LAM) and ornithine 4, 5-aminomutase (4, 5-OAM) are two of
the rare enzymes that use assistance of two vitamins as cofactors. These enzymes employ …
the rare enzymes that use assistance of two vitamins as cofactors. These enzymes employ …
Role of active site residues in promoting cobalt–carbon bond homolysis in adenosylcobalamin-dependent mutases revealed through experiment and computation
GD Román-Meléndez, P von Glehn, JN Harvey… - Biochemistry, 2014 - ACS Publications
Adenosylcobalamin (AdoCbl) serves as a source of reactive free radicals that are generated
by homolytic scission of the coenzyme's cobalt–carbon bond. AdoCbl-dependent enzymes …
by homolytic scission of the coenzyme's cobalt–carbon bond. AdoCbl-dependent enzymes …
Spectroscopic and computational studies of cobalamin species with variable lower axial ligation: Implications for the mechanism of Co–C bond activation by class I …
KS Conrad, CD Jordan, KL Brown… - Inorganic …, 2015 - ACS Publications
5′-deoxyadenosylcobalamin (coenzyme B12, AdoCbl) serves as the cofactor for several
enzymes that play important roles in fermentation and catabolism. All of these enzymes …
enzymes that play important roles in fermentation and catabolism. All of these enzymes …
A mechanochemical switch to control radical intermediates
E Brunk, WF Kellett, NGJ Richards… - Biochemistry, 2014 - ACS Publications
B12-dependent enzymes employ radical species with exceptional prowess to catalyze some
of the most chemically challenging, thermodynamically unfavorable reactions. However …
of the most chemically challenging, thermodynamically unfavorable reactions. However …
Dynamic, electrostatic model for the generation and control of high-energy radical intermediates by a coenzyme B12-dependent enzyme
ZG Chen, MA Ziętek, HJ Russell, S Tait, S Hay… - …, 2013 - pmc.ncbi.nlm.nih.gov
High-energy radical species are widespread in biology as transient reaction intermediates
and free radicals. The control of these extremely reactive molecules is crucial to limit …
and free radicals. The control of these extremely reactive molecules is crucial to limit …
Electron Spin Echo Envelope Modulation Spectroscopy Reveals How Adenosylcobalamin-Dependent Lysine 5, 6-Aminomutase Positions the Radical Pair …
JR Chen, TX Ke, PA Frey, SC Ke - ACS Catalysis, 2021 - ACS Publications
Electron spin echo envelope modulation (ESEEM) spectroscopy reveals several interactions
that serve to weaken the Co–C5′ bond, through stabilization of the cleaved state, thereby …
that serve to weaken the Co–C5′ bond, through stabilization of the cleaved state, thereby …
Quantum Mechanics/Molecular Mechanics Studies on the Mechanism of Action of Cofactor Pyridoxal 5′‐Phosphate in Ornithine 4, 5‐Aminomutase
A computational study was performed on the experimentally elusive cyclisation step in the
cofactor pyridoxal 5′‐phosphate (PLP)‐dependent d‐ornithine 4, 5‐aminomutase (OAM) …
cofactor pyridoxal 5′‐phosphate (PLP)‐dependent d‐ornithine 4, 5‐aminomutase (OAM) …