Rearrangements of organic peroxides and related processes

• Ivan A. Yaremenko,
• Vera A. Vil’,
• Dmitry V. Demchuk and
• Alexander O. Terent’ev

Beilstein J. Org. Chem. 2016, 12, 1647–1748, doi:10.3762/bjoc.12.162

Organic chemistry meets polymers, nanoscience, therapeutics and diagnostics

• Vincent M. Rotello

Beilstein J. Org. Chem. 2016, 12, 1638–1646, doi:10.3762/bjoc.12.161

• just starting to move into nanoparticles. As with the polymers, we started off studying the interactions of recognition element-functionalized nanoparticles with monovalent guests – in this case our old friend flavin where we showed modulation of the flavin redox potentials [21]. Taking this research

• one step further, we created a nanoparticle with a mixed monolayer consisting of hydrogen bonding and aromatic staking sidechains. When we incubated this NP with flavin we observed an increase in binding over time, i.e., we were able to template the particle to the guest [22]. We have since

• with our rather neurotic Weimaraner Trudy, allowing us to get double duty from our toil. Flavoenzyme model system for determining the role of aromatic stacking in flavin redox processes. Reprinted with permission from [10]. Copyright (1997) American Chemical Society. Recognition element-functionalized

Biosynthesis of oxygen and nitrogen-containing heterocycles in polyketides

• Franziska Hemmerling and
• Frank Hahn

Beilstein J. Org. Chem. 2016, 12, 1512–1550, doi:10.3762/bjoc.12.148

• that already at the stage of the first post-PKS modifications, the alnumycin (37) pathway differs from the above mentioned routes (Scheme 8). Prior to pyran cyclisation, the lateral ring of precursor 48 is hydroxylated by the combined action of the two-component flavin-containing monooxygenase (FMO

• ) AlnT and the flavin reductase AlnH [33]. No 3HAD homolog is present in the gene cluster that could catalyse a similar reaction as in the above mentioned examples. Instead, the oxidoreductase AlnO was proposed to catalyse the stereoselective reduction of the ketone at C15 in 49. The pyran 51 would then

• any cofactors, in spite of its flavin adenine dinucleotide (FAD) binding site [98][99]. The reaction mechanisms and biosynthetic enzymes involved in the rearrangement of versicolorin B (106) to demethylsterigmatocystin (107) have also been discussed controversely. Up to four genes (aflM, aflN, aflX

Cyclisation mechanisms in the biosynthesis of ribosomally synthesised and post-translationally modified peptides

• Andrew W. Truman

Beilstein J. Org. Chem. 2016, 12, 1250–1268, doi:10.3762/bjoc.12.120

• McbD, respectively, for microcin B17) that cooperate to catalyse heterocyclisation of specific serine and cysteine residues in McbA, and a flavin-dependent dehydrogenase (the “B-protein”, McbC for microcin B17) that oxidises these heterocycles. These early in vitro studies indicated that the “C-protein

• oxidatively decarboxylated cysteine residue onto a Dha residue derived from serine (Figure 5A). Extensive in vitro experiments indicate that decarboxylation of cysteine precedes 1,4-addition and is catalysed by a flavoprotein (EpiD) in epidermin biosynthesis [66][67], which uses flavin mononucleotide (FMN) to

Photo, thermal and chemical degradation of riboflavin

• Muhammad Ali Sheraz,
• Sadia Hafeez Kazi,
• Sofia Ahmed,
• Zubair Anwar and
• Iqbal Ahmad

Beilstein J. Org. Chem. 2014, 10, 1999–2012, doi:10.3762/bjoc.10.208

• processes and is known to transfer single electrons, hydrogen atoms and hydride ions to a substrate. In this way it may contribute in redox reactions as either a one- or two-electron mediator thus proving itself as a necessary molecule for the flavin-dependent enzymatic reactions in biological systems. The

• two major coenzymes, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), account for the vitamin activity in human nutrition [13]. RF is among the most widely studied compounds in terms of photostability and degradation in aqueous and organic solvents. It shows strong absorption at 223

• excited triplet state of RF [24][36][59] whereas the excited singlet state plays a role in the formation of LC and CDRF [14][24][35][42]. The excitation of the RF molecule on the absorption of light takes place very rapidly as the life spans of flavin excited singlet and triplet states are approximately 5

Intermediates in monensin biosynthesis: A late step in biosynthesis of the polyether ionophore monensin is crucial for the integrity of cation binding

• Wolfgang Hüttel,
• Jonathan B. Spencer and
• Peter F. Leadlay

Beilstein J. Org. Chem. 2014, 10, 361–368, doi:10.3762/bjoc.10.34

• a transferase (MonKSX) transfers the chain to a discrete acyl carrier protein (MonACPX) [20], both of these proteins being encoded within the monensin gene cluster [16]. The flavin-dependent epoxidase MonCI then catalyses three stereospecific epoxidations to give the tri-epoxide 3, which then

Mutational analysis of a phenazine biosynthetic gene cluster in Streptomyces anulatus 9663

• Orwah Saleh,
• Katrin Flinspach,
• Lucia Westrich,
• Andreas Kulik,
• Bertolt Gust,
• Hans-Peter Fiedler and
• Lutz Heide

Beilstein J. Org. Chem. 2012, 8, 501–513, doi:10.3762/bjoc.8.57

• are mobile electron carriers containing a flavin mononucleotide as the prosthetic group and mediating redox processes among a promiscuous set of donors and acceptors. For unknown reasons, the individual deletion of ppzU from cosmid ppzOS04 was unsuccessful. However, we did succeed in the deletion of

Reduction of benzylic alcohols and α-hydroxycarbonyl compounds by hydriodic acid in a biphasic reaction medium

• Michael Dobmeier,
• Josef M. Herrmann,
• Dieter Lenoir and
• Burkhard König

Beilstein J. Org. Chem. 2012, 8, 330–336, doi:10.3762/bjoc.8.36

• deoxygenated product into the the more highly substitued, thermodynamically more stable alkene occurred. Propargylic alcohols (Table 2, entry 3 and 4) showed elimination or decomposed. In the case of flavin (Table 2, entry 6), three hydroxy groups were reduced and one was converted into an iodo substituent

Synthesis of rigidified flavin–guanidinium ion conjugates and investigation of their photocatalytic properties

• Harald Schmaderer,
• Mouchumi Bhuyan and
• Burkhard König

Beilstein J. Org. Chem. 2009, 5, No. 26, doi:10.3762/bjoc.5.26

• Harald Schmaderer Mouchumi Bhuyan Burkhard Konig Institute of Organic Chemisty, University of Regensburg, Universitätsstr. 31, D-93040 Regensburg, Germany 10.3762/bjoc.5.26 Abstract Flavin chromophores can mediate redox reactions upon irradiation by blue light. In an attempt to increase their

• catalytic efficacy, flavin derivatives bearing a guanidinium ion as oxoanion binding site were prepared. Chromophore and substrate binding site are linked by a rigid Kemp’s acid structure. The molecular structure of the new flavins was confirmed by an X-ray structure analysis and their photocatalytic

• activity was investigated in benzyl ester cleavage, nitroarene reduction and a Diels–Alder reaction. The modified flavins photocatalyze the reactions, but the introduced substrate binding site does not enhance their performance. Keywords: flavin; guanidine; Kemp’s acid; photocatalysis; template

Towards practical biocatalytic Baeyer- Villiger reactions: applying a thermostable enzyme in the gram- scale synthesis of optically- active lactones in a two-liquid- phase system

• Frank Schulz,
• François Leca,
• Frank Hollmann and
• Manfred T. Reetz

Beilstein J. Org. Chem. 2005, 1, No. 10, doi:10.1186/1860-5397-1-10

• to the best of our knowledge is unprecedented for flavin-dependent monooxygenases in the presence of organic solvents (Table 2). P3-PAMO was found to be active for more than ten hours in the reaction without any loss of activity (Figure 3) and to exhibit reaction rates that correspond to those that

• . We compared the system developed in this study to an analogous synthetic organocatalyst for the enantioselective BV-oxidation as described by Murahashi et al. in 2002.[13] The Murahashi system is related to PAMO because it also uses a flavin-derived catalyst within a chiral environment. Of course