Good vibrations in enzyme-catalysed reactions

S Hay, NS Scrutton - Nature chemistry, 2012 - nature.com
Fast motions (femtosecond to picosecond) and their potential involvement during enzyme-
catalysed reactions have ignited considerable interest in recent years. Their influence on …

Biocatalytic reductions and chemical versatility of the old yellow enzyme family of flavoprotein oxidoreductases

HS Toogood, JM Gardiner, NS Scrutton - ChemCatChem, 2010 - Wiley Online Library
The old yellow enzyme (OYE) family is a large group of flavin‐dependent redox biocatalysts
with major applications in the industrial reduction of activated alkenes. These enzymes have …

A 21st century revisionist's view at a turning point in enzymology

ZD Nagel, JP Klinman - Nature chemical biology, 2009 - nature.com
Despite the fact that the number of publications associated with the keyword'enzyme'
increases every year, the precise origin of enzyme catalysis has remained unresolved …

Old yellow enzyme-catalysed asymmetric hydrogenation: linking family roots with improved catalysis

A Scholtissek, D Tischler, AH Westphal… - Catalysts, 2017 - mdpi.com
Asymmetric hydrogenation of activated alkenes catalysed by ene-reductases from the old
yellow enzyme family (OYEs) leading to chiral products is of potential interest for industrial …

Decoupling of catalysis and transition state analog binding from mutations throughout a phosphatase revealed by high-throughput enzymology

CJ Markin, DA Mokhtari, S Du… - Proceedings of the …, 2023 - National Acad Sciences
Using high-throughput microfluidic enzyme kinetics (HT-MEK), we measured over 9,000
inhibition curves detailing impacts of 1,004 single-site mutations throughout the alkaline …

Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'‐reductase related to old yellow enzyme

BV Adalbjörnsson, HS Toogood… - …, 2010 - Wiley Online Library
We report the crystal structure of a thermophilic “ene” reductase (TOYE) isolated from
Thermoanaerobacter pseudethanolicus E39. The crystal structure reveals a tetrameric …

Hydrogen donor–acceptor fluctuations from kinetic isotope effects: A phenomenological model

D Roston, CM Cheatum, A Kohen - Biochemistry, 2012 - ACS Publications
Kinetic isotope effects (KIEs) and their temperature dependence can probe the structural
and dynamic nature of enzyme-catalyzed proton or hydride transfers. The molecular …

Direct Analysis of Donor− Acceptor Distance and Relationship to Isotope Effects and the Force Constant for Barrier Compression in Enzymatic H-Tunneling Reactions

CR Pudney, LO Johannissen, MJ Sutcliffe… - Journal of the …, 2010 - ACS Publications
The role of dynamical effects in enzyme catalysis is both complex and widely debated.
Understanding how dynamics can influence the barrier to an enzyme catalyzed reaction …

Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction

CR Pudney, S Hay, C Levy, J Pang… - Journal of the …, 2009 - ACS Publications
In recent years there has been a shift away from transition state theory models for H-transfer
reactions. Models that incorporate tunneling as the mechanism of H-transfer are now …

Deep tunneling dominates the biologically important hydride transfer reaction from NADH to FMN in morphinone reductase

J Pang, S Hay, NS Scrutton… - Journal of the American …, 2008 - ACS Publications
The temperature dependence of the primary kinetic isotope effect (KIE), combined
temperature− pressure studies of the primary KIE, and studies of the α-secondary KIE …