Reactions of 3H-1,2-benzodithiol-3-one 1-oxide with amines and anilines

Kim, Woongki; Dannaldson, Jeffrey; Gates, Kent S.

doi:10.1016/0040-4039(96)01124-0

Cited by 34 publications

(24 citation statements)

References 20 publications

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“…Bond lengths and angles of the benzisothiazolone ring system (Table 1) are in good agreement with the values quoted in a previous report (Kim et al, 1996). The benzisothiazolone ring system is planar, with a maximum deviation from the mean plane of 0.038 (2) Å for atom N1.…”

Section: Commentsupporting

confidence: 90%

2-(Hydroxymethyl)-1,2-benzothiazol-3(2H)-one

Lin

Yin

2006

Acta Cryst E

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Section: Commentsupporting

confidence: 90%

2-(Hydroxymethyl)-1,2-benzothiazol-3(2H)-one

Lin

Yin

2006

Acta Cryst E

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“…Interestingly, examples of cyclic sulfenamides were reported some 30 years ago in studies of the synthesis of the antibiotic cephalosporin from penicillin precursors via the nucleophilic attack of a nitrogen atom on sulfenic acids (26)(27)(28). More recently, the synthesis of a cyclic sulfenamide species in vitro from a sulfenic acid precursor was demonstrated (29).…”

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confidence: 99%

Reversible Oxidation of the Membrane Distal Domain of Receptor PTPα Is Mediated by a Cyclic Sulfenamide

et al. 2006

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Protein tyrosine phosphatases (PTPs) are fundamental to the regulation of cellular signalling cascades triggered by protein tyrosine kinases. Most receptor-like PTPs (RPTPs) comprise two tandem PTP domains, with only the membrane proximal domains (D1) having significant phosphatase activity; the membrane distal domains (D2) display little to no catalytic activity. Intriguingly, however, many RPTP D2s share the catalytically essential Cys and Arg residues of D1s. D2 of RPTPR may function as a redox sensor that mediates regulation of D1 via reactive oxygen species. Oxidation of Cys723 of RPTPR D2 (equivalent to PTP catalytic Cys residues) stabilizes RPTPR dimers, induces rotational coupling, and is required for inactivation of D1 phosphatase activity. Here, we investigated the structural consequences of RPTPR D2 oxidation. Exposure of RPTPR D2 to oxidants promotes formation of a cyclic sulfenamide species, a reversibly oxidized state of Cys723, accompanied by conformational changes of the D2 catalytic site. The cyclic sulfenamide is highly resistant to terminal oxidation to sulfinic and sulfonic acids. Conformational changes associated with RPTPR D2 oxidation have implications for RPTPR quaternary structure and allosteric regulation of D1 phosphatase activity.The reversible tyrosine phosphorylation of proteins, reciprocally controlled by tyrosine kinases and phosphatases, is crucial to the regulation of diverse cellular processes, including growth, proliferation, and differentiation (1). Redox reactions, mediated by reactive oxygen species (ROS), 1 control PTP activity in response to a variety of hormones and growth factors (2-6). Generation of ROS accompanies PTK activation (7,8), with oxidation-induced inhibition of PTP activity amplifying PTK-dependent signaling (9-11).PTP-catalyzed protein dephosphorylation proceeds via a nucleophilic displacement reaction utilizing an essential cysteine residue conserved within the PTP signature motif Cys(X) 5 Arg (12-15). The low pK a of the catalytic cysteine necessary for its function (16) renders PTPs susceptible to inactivation by ROS-induced cysteine oxidation. However, the reversibility of redox-mediated inactivation of PTPs requires that a reversibly oxidized state of the cysteine residue be stabilized at the PTP catalytic site and that formation of SO 2 and SO 3 , two irreversibly oxidized species of cysteine, be suppressed (17). Crystallographic studies of the tyrosine specific cytosolic PTP1B revealed that the reversibly oxidized form of the enzyme was not the expected sulfenic acid or disulfide bond, but an oxidation state of cysteine termed a cyclic sulfenamide, a species not previously observed in proteins (18,19). Generation of the cyclic sulfenamide inhibits catalytic activity by blocking the nucleophilic cysteine residue through a covalent bond of its thiol group with the neighboring main chain amide, a linkage that is accompanied by profound conformational transitions of the catalytic site PTP and pTyr loops. The oxidation properties of the catalyt...

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“…A search of the Cambridge Structural Database (CSD; Version 5.31; Allen 2002) for phenylthiolate fragments C 6 H 5Ày SX (X = SO 2 C 6 H 5Ày ; y = 0, 1) yielded seven structures: benzenethiosulfonic acid phenyl ester (CSD refcode BILCII10; Caputo et al, 1984), S-(p-tolyl) p-toluenethiosulfonate (refcode BILCOO01; Ferguson et al, 2000), p-tolylthiosulfonic acid p-tolyl ester (refcode BILCOO10; Caputo et al, 1984), di(p-bromophenyl) thiosulfonate (refcode BPTSLF; Noordik & Vos, 1967), S-(2-nitrophenyl) 2-nitro-benzenethiosulfonate (refcode FUQMIN; Glidewell et al, 2000), S-(2-nitrophenyl) p-toluenethiosulfonate (refcode LIYQOZ; and bis Ndipropylcarbamoyl)phenyl] thiosulfinate (refcode NAJBIJ; Kim et al, 1996), with an average S-SO 2 distance of 2.087 (4) Å (restraints used in the search: only three-dimensional coordinates available; no private communication; only one sulfone group and no cyclic disulfide). The O-S-O angle is much larger than the ideal tetrahedral values, doubtless as a consequence of both the substantial negative charge on the geminal O atoms (Table 1), which is observed also in (II) as well as in the seven compounds found in the search of the CSD described above, and the -bonding/double S O bonds.…”

Section: Figurementioning

confidence: 99%

S-(4-Nitrophenyl) 4-nitrobenzenethiosulfonate

et al. 2010

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The title compound, C(12)H(8)N(2)O(6)S(2), (I), is a positional isomer of S-(2-nitrophenyl) 2-nitrobenzenethiosulfonate [Glidewell, Low & Wardell (2000). Acta Cryst. B56, 893-905], (II). The most obvious difference between the two isomers is the rotation of the nitro groups with respect to the planes of the adjacent aryl rings. In (I), the nitro groups are only slightly rotated out of the plane of the adjacent aryl ring [2.4 (6) and 6.7 (7) degrees ], while in (II) the nitro groups are rotated by between 37 and 52 degrees , in every case associated with S-S-C-C torsion angles close to 90 degrees . Other important differences between the isomers are the C-S-S(O(2))-C torsion angle [78.39 (2) degrees for (I) and 69.8 (3) degrees for (II) (mean)] and the dihedral angles between the aromatic rings [12.3 (3) degrees for (I) and 28.6 (3) degrees for (II) (mean)]. There are two types of C-H...O hydrogen bond in the structure [C...O = 3.262 (7) A and C-H...O = 144 degrees ; C...O = 3.447 (7) A and C-H...O = 166 degrees ] and these link the molecules into a two-dimensional framework. The hydrogen-bond-acceptor properties differ between the two isomers.

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Reactions of 3H-1,2-benzodithiol-3-one 1-oxide with amines and anilines

Cited by 34 publications

References 20 publications

2-(Hydroxymethyl)-1,2-benzothiazol-3(2H)-one

2-(Hydroxymethyl)-1,2-benzothiazol-3(2H)-one

Reversible Oxidation of the Membrane Distal Domain of Receptor PTPα Is Mediated by a Cyclic Sulfenamide

S-(4-Nitrophenyl) 4-nitrobenzenethiosulfonate

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