The chemistry of 2,1-benzisothiazoles. IX. The reaction of 3-chloro-substituted 2,1-benzisothiazoles with nucleophiles and the preparation of(2,1-Benzisothiazol-3-yl)acetic acid

Davis, Michael; Homfeld, E.; Mcvicars, Jill; Pogany, S

doi:10.1071/ch9752051

Cited by 4 publications

(2 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2-Naphthylmethylselenideacetic acid, a(+)-2,4,5-trichlorophenoxypropionic acid, and a(-)-2,4,5-trichlorophenoxypropionic acid were generously supplied by Professor B. Aberg, Vaxtfysiologiska Institutionen, Lantbrukshogskolan, Uppsala, Sweden. Benzisothiazoles, synthesized by the procedures by Davis et al (13) (Table III). The m-and o-isomers of nitrophenylacetic acid are auxins but p-nitrophenylacetic acid is inactive as an auxin (3,9) and thus the ligand specificity of ABP qualitatively correlates with the biological activity of these phenylacetic acid derivatives.…”

mentioning

confidence: 99%

“…While TIBA and a-NPA have comparable activities as inhibitors of IAA transport in bean petioles (20), the affinity of ABP for TIBA is an order of magnitude greater than that for a-NPA (Table VII). It (1,2-Benzisothiazol-3-yl)-acetic acid is a strong auxin (7) and a variety of benzisoxazole and benzisothiazole derivatives are also active auxins (13,17). (2,1-Benzisothiazo-3-yl)-carboxylic acid (Cro: 8 x l0-7 M) is a strong inhibitor of IAA-binding, whereas the corresponding methyl ester is ineffective.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Ligand Specificity of Bean Leaf Soluble Auxin-binding Protein

Wardrop¹,

Polya²

1980

Plant Physiol.

View full text Add to dashboard Cite

The soluble bean leaf auxin-binding protein (ABP) has a high affinity for a range of auxins including indole-3-acetic acid (IAA), a-napthaleneacetic acid, phenylacetic acid, 2,4,5-trichlorophenoxyacetic acid, and structurally related auxins. A large number of nonauxin compounds that are nevertheless structurally related to auxins do not displace IAA from bean ABP. Bean ABP has a high affinity for auxin transport inhibitors and antiauxins. The specificity of pea ABP for representative auxins is similar to that found for bean ABP. The bean ABP auxin binding site is similar to the corn endoplasmic reticulum auxin-binding sites in specificity for auxins and sensitivity to thiol reagents and azide. Qualitative similarities between the ligand specificity of bean ABP and the specificity of auxin-induced bean leaf hyponasty provide further evidence, albeit circumstantial, that ABP (ribulose 1,5-bisphosphate carboxylase) can bind auxins in vivo. The high incidence of ABP in bean leaves and the high affity of this protein for auxins and auxin transport inhibitors suggest possible functions for ABP in auxin transport and/or auxin sequestration.We have presented evidence for the identity of the high incidence, soluble ABPs2 of bean and pea leaves with RuBPCase (32).Because the (NH4)2SO4 precipitation assay for IAA-ABP binding is highly reproducible and the basis for lack of IAA-binding by some ABP preparations in equilibrium dialysis is not known (32), the former procedure has been employed to examine the ligand specificity of ABP. This approach can provide the ligand specificity of a model high affmity ABP-and in addition will define the nature of a major plant auxin-binding site if the in vitro results directly reflect the behavior of an active conformer of ABP (RuBPCase) in vivo. We have shown previously (31) that the partially purified bean leaf ABP binds a variety of active synthetic auxins. The present paper describes the interaction of extensively purified bean leaf ABP with a wide range of naturally occurring and synthetic auxins, antiauxins, auxin transport inhibitors, and structurally related compounds. The binding of representative auxins to purified pea ABP is also reported.MATERIALS AND METHODS Purification of ABP. Bean leaf ABP was purified from about 10-day-old primary leaves of dwarf beans (Phaseolus vulgaris var.

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

Ligand Specificity of Bean Leaf Soluble Auxin-binding Protein

Wardrop¹,

Polya²

1980

Plant Physiol.

View full text Add to dashboard Cite

show abstract

ChemInform Abstract: CHEMISTRY OF 2,1‐BENZISOTHIAZOLES PART 9, REACTION OF 3‐CHLORO‐SUBSTITUTED 2,1‐BENZISOTHIAZOLES WITH NUCLEOPHILES AND THE PREPARATION OF (2,1‐BENZISOTHIAZOL‐3‐YL)ACETIC ACID

Davis¹,

Homfeld²,

Mcvicars³

et al. 1975

Chemischer Informationsdienst

View full text Add to dashboard Cite

show abstract

Einige bestrahlungsexperimente mit 2, 1‐Benzisothiazolen

Jackson

Schmidt

Hansen

1979

Helvetica Chimica Acta

View full text Add to dashboard Cite

Some Irradiation Experiments with 2, 1‐Benzisothiazoles 2, 1‐Benzisothiazole (1) on irradiation with a mercury high‐pressure lamp in benzene/diethylamine yields, after acetylation, 2‐acetylamino‐benzaldehyde (3; Scheme 1). Similarly, irradiation of 3‐chloro‐2, 1‐benzisothiazole (2) in benzene/diethylamine leads to a mixture of 3‐dimethylamino‐2, 1‐benzisothiazole (6a) and N, N‐diethyl‐thioanthranilamide (7a; Scheme 2). Benzisothiazole 6a, on irradiation, is not transformed into 7a. On the other hand, when 2 is irradiated in methanol a mixture of 3‐methoxy‐2, 1‐benzisothiazole (4a) and methyl anthranilate (5a; Scheme 2) is obtained. In this case, 4a on irradiation in methanol or ethanol also yields 5a. No exchange of the methoxy group in 4a is observed when the irradiation is performed in ethanolic solution. Thus, 2, 1‐benzisothiazoles 1, 2 and 4a react photochemically by N,S‐bond cleavage and hydrogen‐atom abstraction from the solvent (Scheme 3). 3‐Chloro‐2, 1‐benzisothiazole (2) shows a second photoreaction, i.e. nucleophilic exchange of the chloro substituent by methanol or diethyl amine. The latter reaction can also be observed thermally, e.g. in boiling methanol in the presence of methoxide ions.

show abstract

The chemistry of 2,1-benzisothiazoles. IX. The reaction of 3-chloro-substituted 2,1-benzisothiazoles with nucleophiles and the preparation of(2,1-Benzisothiazol-3-yl)acetic acid

Cited by 4 publications

References 0 publications

Ligand Specificity of Bean Leaf Soluble Auxin-binding Protein

Ligand Specificity of Bean Leaf Soluble Auxin-binding Protein

ChemInform Abstract: CHEMISTRY OF 2,1‐BENZISOTHIAZOLES PART 9, REACTION OF 3‐CHLORO‐SUBSTITUTED 2,1‐BENZISOTHIAZOLES WITH NUCLEOPHILES AND THE PREPARATION OF (2,1‐BENZISOTHIAZOL‐3‐YL)ACETIC ACID

Einige bestrahlungsexperimente mit 2, 1‐Benzisothiazolen

Contact Info

Product

Resources

About