Crystallization and preliminary diffraction studies of morphinone reductase, a flavoprotein involved in the degradation of morphine alkaloids [PDF]
, 1997 Morphinone reductase from Pseudomonas putida M10, a flavoprotein involved in the degradation of morphine alkaloids, was purified from an overexpressing strain of Escherichia coli and crystallized using the hanging-drop vapour-diffusion method ...
Bruce, N C +4 more
core +1 more source
Co-Overexpression of RIB1 and RIB6 Increases Riboflavin Production in the Yeast Candida famata
Fermentation, 2022 Riboflavin or vitamin B2 is a water-soluble vitamin and a precursor of flavin coenzymes, flavin mononucleotide, and flavin adenine dinucleotide, which play a key role as enzyme cofactors in energy metabolism.
Yana Petrovska +4 more
doaj +1 more source
Multi-heme Cytochromes in Shewanella oneidensis MR-1:Structures, functions and opportunities [PDF]
, 2015 Multi-heme cytochromes are employed by a range of microorganisms to transport electrons over distances of up to tens of nanometers. Perhaps the most spectacular utilization of these proteins is in the reduction of extracellular solid substrates ...
Brown JP +9 more
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Frontiers in Oncology, 2023 PurposeModern techniques for improved tumor visualization have the aim to maximize the extent of resection during brain tumor surgery and thus improve patient prognosis.
David Reichert +18 more
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Mass spectrometry locates local and allosteric conformational changes that occur on cofactor binding
Nature Communications, 2016 The decarboxylate enzyme Fdc1 requires a prenylated flavin mononucleotide co-factor for activity. Here, the authors use a variety of mass spectrometric techniques to observe the structural changes in this protein in response to co-factor binding.
Rebecca Beveridge +5 more
doaj +1 more source
Production of Vitamin B2 (Riboflavin) by Microorganisms: An Overview
Frontiers in Bioengineering and Biotechnology, 2020 Riboflavin is a crucial micronutrient that is a precursor to coenzymes flavin mononucleotide and flavin adenine dinucleotide, and it is required for biochemical reactions in all living cells.
Liudmila A. Averianova +8 more
doaj +1 more source
The structural and functional basis of catalysis mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans. [PDF]
PLoS ONE, 2014 FerB from Paracoccus denitrificans is a soluble cytoplasmic flavoprotein that accepts redox equivalents from NADH or NADPH and transfers them to various acceptors such as quinones, ferric complexes and chromate.
Vojtěch Sedláček +3 more
doaj +1 more source
Biophysical characterization of folded state type II luciferase‐like monooxygenase
Indonesian Journal of Biotechnology, 2023 We noticed that the Priestia megaterium genome contains five Luciferase‐like monooxygenase (LLM) encoding genes, however, their functions are unknown. The objective of this work was to characterize the biophysical properties of the recombinant LLM2 from ...
Adinda Fitri Salsabila +4 more
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A ternary mechanism for NADH oxidation by positively charged electron acceptors, catalyzed at the flavin site in respiratory complex I [PDF]
, 2011 The flavin mononucleotide in complex I (NADH:ubiquinone oxidoreductase) catalyzes NADH oxidation, O2 reduction to superoxide, and the reduction of several ‘artificial’ electron acceptors.
Birrell, James A. +2 more
core +1 more source
Biomolecules, 2020 Flavin cofactors, like flavin adenine dinucleotide (FAD), are important electron shuttles in living systems. They catalyze a wide range of one- or two-electron redox reactions.
Martina Kieninger +2 more
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