Same substrate, many reactions: oxygen activation in flavoenzymes

E Romero, JR Gómez Castellanos, G Gadda… - Chemical …, 2018 - ACS Publications
Over time, organisms have evolved strategies to cope with the abundance of dioxygen on
Earth. Oxygen-utilizing enzymes tightly control the reactions involving O2 mostly by …

Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts

WJH Van Berkel, NM Kamerbeek, MW Fraaije - Journal of biotechnology, 2006 - Elsevier
During the last decades a large number of flavin-dependent monooxygenases have been
isolated and studied. This has revealed that flavoprotein monooxygenases are able to …

[HTML][HTML] Gates of enzymes

A Gora, J Brezovsky, J Damborsky - Chemical reviews, 2013 - ACS Publications
Enzymes are very efficient catalysts that are essential for the functioning of living organisms.
The low efficiency of biocatalysts produced de novo relative to those that have evolved …

Triepoxide formation by a flavin-dependent monooxygenase in monensin biosynthesis

Q Wang, N Liu, Y Deng, Y Guan, H Xiao… - Nature …, 2023 - nature.com
Monensin A is a prototypical natural polyether polyketide antibiotic. It acts by binding a metal
cation and facilitating its transport across the cell membrane. Biosynthesis of monensin A …

Baeyer–Villiger monooxygenases, an emerging family of flavin‐dependent biocatalysts

NM Kamerbeek, DB Janssen… - Advanced Synthesis …, 2003 - Wiley Online Library
Abstract Baeyer–Villiger monooxygenases (BVMOs) are flavoenzymes that catalyze a
remarkably wide variety of oxidative reactions such as regio‐and enantioselective Baeyer …

Oxygenases as powerful weapons in the microbial degradation of pesticides

M Cheng, D Chen, RE Parales… - Annual Review of …, 2022 - annualreviews.org
Oxygenases, which catalyze the reductive activation of O2 and incorporation of oxygen
atoms into substrates, are widely distributed in aerobes. They function by switching the …

Control of catalysis in flavin-dependent monooxygenases

BA Palfey, CA McDonald - Archives of biochemistry and biophysics, 2010 - Elsevier
Flavoprotein monooxygenases reduce flavins, speed their reaction with oxygen, and
stabilize a C4a-oxygen adduct long enough to use this reactive species to transfer an …

Reconstructing NMR spectra of “invisible” excited protein states using HSQC and HMQC experiments

NR Skrynnikov, FW Dahlquist… - Journal of the American …, 2002 - ACS Publications
Carr− Purcell− Meiboom− Gill (CPMG) relaxation measurements employing trains of 180°
pulses with variable pulse spacing provide valuable information about systems undergoing …

Monooxygenation of aromatic compounds by flavin‐dependent monooxygenases

P Chenprakhon, T Wongnate, P Chaiyen - Protein Science, 2019 - Wiley Online Library
Many flavoenzymes catalyze hydroxylation of aromatic compounds especially phenolic
compounds have been isolated and characterized. These enzymes can be classified as …

Debottlenecking 4-hydroxybenzoate hydroxylation in Pseudomonas putida KT2440 improves muconate productivity from p-coumarate

E Kuatsjah, CW Johnson, D Salvachúa, AZ Werner… - Metabolic …, 2022 - Elsevier
Abstract The transformation of 4-hydroxybenzoate (4-HBA) to protocatechuate (PCA) is
catalyzed by flavoprotein oxygenases known as para-hydroxybenzoate-3-hydroxylases …