Figure 1
Sulfur pathway in the metabolism of several organisms.
Figure 2
Possible mechanism for disulfide reductase. Reprinted with permission from American Chemical Society. (Herwald et al. 2013). Copyright 2015 American Chemical Society.
Figure 3
Oxidation of a sulfide to sulfoxides and sulfone.
Figure 4
Biotin-l-sulfoxide formation from the fermentation using A. niger (Wright et al. 1954b).
Figure 5
Sulfoxides studied by Auret et al. (Auret et al. 1966) (a) and the chemical oxidation with (+)-percamphoric acid described by Montanari (1965) (b).
Figure 6
Production of optical pure sulfoxides with different microorganisms.
Figure 7
Oxidation of 1,3-dithian in the presence of different fungi.
Figure 8
Molecular models of thioanisole, Br-thioanisole and Me-thioanisole in the active site. The amino acid residues that were subjected to mutagenesis are presented in magenta color (V207, F293 and N258). (a) Thioanisole in wild type active site; (b) p-tolyl in wild type active site, (c) Br-thioanisole in wild-type active site, (d) Br-thioanisole in F293H, (e) p-tolyl in V207A modified enzyme and (f) p-tolyl in V207I modified enzyme. Reprinted with permission from Oxoford University Press. (Shainsky et al. 2013) Copyright 2015 Oxford University Press.
Figure 9
Top perspective view of the active site model showing the preferred binding modes for phenyl alkyl sulfides. Reprinted with permission from Elsevier (Ottolina et al. 1995). Copyright 2015 Elsevier.
Figure 10
Binding model for substrates bearing large alkyl groups. (Holland et al. 1997b) Reprinted with permission from Elsevier (Holland et al. 1997b). Copyright 2015 Elsevier.
Figure 11
Binding model for substrates bearing small alkyl groups (Holland et al. 1997b). Reprinted with permission from Elsevier (Holland et al. 1997b). Copyright 2015 Elsevier.
Figure 12
Sulfide oxidation using P. frederiksbergensis strains.
Figure 13
Use of several Aspergillus strains as biocatalysts for the oxidation of cyclohexyl(methyl)sulfide and alkyl aryl sulfide.
Figure 14
NADPH regeneration system in the oxidation of para-chloro-thioanisole by recombinant E. coli BL21 (pET28a-P450-GDH).
Figure 15
Sulfoxides prepared from reactions with flavin-containing monooxygenase (FMO), fused to phosphite dehydrogenase (Rioz-Martinez et al. 2011).
Figure 16
Use of BVMOs (HAPMO, M-PAMO and PAMO) described by Rioz-Martínez et al. (2010) to produce sulfoxides.
Figure 17
Several sulfoxides prepared from oxidations with Dietzia sp.
Figure 18
Deoxygenation of racemic sulfoxide by Rhodobacter sphaeroides f. sp. denitrificans (Abo et al. 1997).
Figure 19
Substrates used by Hanlon et al. (1998) for deoxygenation with dimethyl sulfoxide reductase.
Figure 20
Substrates for enantiomeric enrichment via deoxygenation using DMSO reductase from Citrobacter braakii.
Figure 21
Transformation of δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine into isopenicillin N.
Figure 22
Oxidation of benzothiophene derivatives by Pseudomonas sp. BT1.
Figure 23
Oxidation of benzothiophene with Pseudomonas putida RE204.
Figure 24
Dioxygenase-catalysed oxidation of 2-MB[b]T.
Figure 25
Thiophene over oxygenation and formation of cycloadducts.
Figure 26
Thiosulfinates obtained by sulfoxidation of 1,2-disulfides.
Figure 27
Sulfoxidation of 1,3-disulfides mediated by TDO and NDO.
Figure 28
Oxidation of 4,6-dimethyl dibenzothiophene by CPO immobilized on silica-based materials. (Montiel et al. 2007).
Figure 29
Microbial desulfurization of DBT.
Figure 30
Oxidation of thiocarbamate herbicides by liver enzymes.
Figure 31
Esomeprazole sulfide and other related compounds used as substrates for biooxidations with Lysinibacillus sp. B71 (Babiak et al. 2011).
Figure 32
Oxidation of Cephalosporin G, Penicillin G and Penicillin V.
Figure 33
Pathway for the pepsin-catalyzed hydrolysis of sulfite esters described by Stein and Fahrn (1968).
Figure 34
Substrates used in the hydrolysis reaction by pepsin.
Figure 35
Reactions of thiols with vinyl esters catalyzed by lipase, CAL-B: Markovnikov product (a) and anti-Markovnikov product (b).
Figure 36
Addition of nucleophiles to α,β-unsaturated sulfinyl derivatives using hydrolytic enzymes. Figure adapted with permission from Elsevier (Madalinska et al. 2012).
Figure 37
Use of alkylsulfatase Pisa 1 to obtain a mixture of sec-alcohol and non-reacted sulfate ester.
Figure 38
Chemo-enzymatic synthesis of methyl parathion and its oxon.
Figure 39
Nitrogen transfer reaction using P450 enzymes.
Figure 40
Selenium metabolism pathway in animals.
Figure 41
Oxidation of benzyl(p-tolyl)selane with A. niger.
Figure 42
Incubation of a series of phenyl selenides with Aspergillus niger, Aspergillus foetidus, Mortierella isabellina and Helminthosporium sp.
Figure 43
α-Phenylselenoacrolein formation using cyclohexanone oxygenase.
Figure 44
Oxidation of Ebselen (a) and 2-(Methylseleno)benzanilide (b) catalyzed by FMO1 (Ziegler et al. 1992).
Figure 45
Biomethylation reaction of (S)-1-(phenylseleno)-2-propanol.
Figure 46
Kinetic Resolution of aromatic selenides using BVMOs as biocatalysts.
Figure 47
Transport and absorption of borate in a cell.
Figure 48
Oxidation of boronic acids by cyclohexanone oxygenase.
Figure 49
Oxidation of boron-containing acetophenones by Baeyer-Villiger Monooxygenases.
Figure 50
Oxidation of chiral boranes to alcohols by BVMO.
Figure 51
Reactions of several organoboron compounds with BVMOs.
Figure 52
Phosphorus uptake and its metabolic pathway.
Figure 53
Bialaphos biosynthesis.
Figure 54
Crotoxyphos degradation by hydrolases.
Figure 55
Trypsin-catalyzed siloxane bond formation.
Figure 56
Enzyme-catalyzed siloxane bond formation.
Figure 57
Screening of enzymes for siloxane bond formation in aqueous or organic solvent media.
Figure 58
A proposed mechanism for hydrolase-catalyzed silanol condensation.
Figure 59
Enzyme-catalyzed transetherification and/or alcohol-silanol condensation.
Figure 60
Lipase-catalyzed transesterification/transetherification reactions.
