Electrochemical studies of adrenergic neurotrans-mitters and related compounds

Sternson, Arlene W.; McCreery, Richard L.; Feinberg, Benjamin A.; Adams, Ralph N.

doi:10.1016/s0022-0728(73)80139-1

Cited by 169 publications

(93 citation statements)

References 12 publications

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“…With eight ⑀-amino and three thiol equivalents/mol, the protein is well endowed with reactive side chains. Thiols are up to 4000 times more reactive than amines in the nucleophilic attack of quinones (19,27) formed by the oxidation of peptidyl-Dopa. The participation of thiols in protein cross-linking was explored by hydrolyzing plaque footprints and screening for Dopa adducts by affinity chromatography on phenylboronate.…”

Section: Discussionmentioning

confidence: 99%

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Linking Adhesive and Structural Proteins in the Attachment Plaque of Mytilus californianus

Zhao

Waite

2006

Journal of Biological Chemistry

248

243

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The byssal attachment of California mussels Mytilus californianus provides secure adhesion in the presence of moisture, a feat that still eludes most synthetic polymers. Matrix-assisted laser desorption ionization mass spectrometry was used to probe the footprints of byssal attachment plaques on glass cover slips for adhesive proteins. Besides the abundant mcfp-3 protein family (Zhao, H., Robertson, N. B., Jewhurst, S. A., and Waite, J. H. (2006) J. Biol. Chem. 281, 11090 -11096), two new proteins, mcfp-5 and mcfp-6, with masses of 8.9 kDa and 11.6 kDa, respectively, were identified in footprints, partially characterized and completely sequenced from a cDNA library. mcfp-5 resembles mcfp-3 in its basic pI and abundant 3,4-dihydroxyphenyl-L-alanine (Dopa; 30 mol %), but is distinct in two respects: it is more homogeneous in primary sequence and is polyphosphorylated. mcfp-6 is basic and contains a small amount of Dopa (<5 mol %). In contrast to mcfp-3 and -5, tyrosine prevails at 20 mol %, and cysteine is present at 11 mol %, one-third of which remains thiolate. Given the oxidative instability of Dopa and cysteine at pH 8.2 (seawater), we tested the hypothesis that thiols serve to scavenge dopaquinones by adduct formation. Plaque footprints were hydrolyzed and screened for cysteine dopaquinone adducts using phenylboronate affinity chromatography. 5-S-Cysteinyldopa was detected at nearly 1 mol %. The results suggest that mcfp-6 may provide a cohesive link between the surface-coupling Dopa-rich proteins and the bulk of the plaque proteins.Mussels inhabit wind and wave swept rocky seashores. Such habitats are deathtraps for exposed organisms lacking a secure attachment. Accordingly, mussels have evolved a robust holdfast known as the byssus, which is essentially a specialized 4 -5-cm long bundle of collagenous fibers that is proximally rooted in the mussel and distally bonded to foreign surfaces underwater by flattened attachment plaques (1).Given that engineering durable adhesive bonds between minerals and organic polymers in the presence of moisture remains a serious technological challenge, fundamental insights into the mechanism of holdfast adhesion in mussels and other sessile marine organisms represent a potential data base of bio-inspired solutions to the moisture problem (1). One popular technique for improving "wet" adhesion on siliceous substrates involves the application of surface-coupling agents or adhesion promoters (2). Organosilanes are the best known synthetic adhesion promoters and typically designed with specific moieties for silica ligation at one end and reactivity toward the organic polymer at the other (2).The use of surface-coupling agents to promote adhesion resonates with the adhesive biochemistry of byssal plaques made by mussels. A recent investigation of plaque footprints in Mytilus californianus has revealed a family of protein variants (mcfp-3) with a 3,4-dihydroxyphenyl-L-alanine (Dopa) 2 content that approaches 25 mol % (3, 4). With its many Dopa residues, mcfp-3 has been compared wi...

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Section: Discussionmentioning

confidence: 99%

“…7). The last of these is the fastest and surest of the three (19) and would provide an important link between the proteins at the surface and interior of the plaque.…”

Section: Discussionmentioning

confidence: 99%

Linking Adhesive and Structural Proteins in the Attachment Plaque of Mytilus californianus

Zhao

Waite

2006

Journal of Biological Chemistry

248

243

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“…The first possibility is the reaction of the o-quinone with water (reaction [1]) o II OH cr [2] ~ OH This species may then undergo a polymerization reaction (15). Alternatively, the o-quinone can react with the starting material, as shown in reaction [3] [3a]…”

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confidence: 99%

The Electrochemical Oxidation of Substituted Catechols

Ryan

Yueh

Chen

1980

J. Electrochem. Soc.

202

115

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The oxidation of substituted catechols was studied by cyclic voltammetry, chronoamperometry, rotating ring‐disk electrode, and coulometry. The results showed that the quinones that were formed from the oxidation of substituted catechols reacted with the basic forms of the starting material to yield the dimeric product. These products were generally unstable and rapidly polymerized or underwent some other irreversible reaction to form an electroinactive product. For 3,4‐dihydroxyacetophenone and propriophenone, the intermediate was stable long enough to be observed in cyclic voltammetry. The rate of the coupling reaction was found to correlate well with the Hammett ρ‐σ parameters and indicated that there was substantial negative charge in the transition state. Finally, an analysis of the coulometric n‐values along with the inormalat1/2/C values indicated that the initial coupling product was a diphenyl ether. Analysis of the coulometry products showed extensive polymerization.

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“…Electrochemical oxidation of o-and p-diphenols has been studied by several researchers. [2,3] O-and p-quinines produced by oxidation of o-and p-catechols are unstable compounds, and can be used as an acceptor in the Micheleaddition reaction, which undergo attacks by nucleophiles such as 5-methyl-2-mercapto-1,3,4-thiadiazole, [4] 1,3-diethyl-2-thiobarbituric acid, [5] Meldrum's acid, [6] cyanoacetone, [7] and 3-hydroxy-1H-phenalene-1-one. [8] Thiouracils are minor components of transfer-RNA, have anti-herpes virus activities, and have been used for the treatment of hyperthyroidism in men.…”

Section: Introductionmentioning

confidence: 99%

Clean and Green Synthesis of New Benzothiazole Derivatives via Electrochemical Oxidation of Catechol Derivatives

Chamjangali¹,

Daneshinejad²,

Bakherad³

et al. 2016

Croat. Chem. Acta

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Electrochemical oxidation of the catechols 1a and 1b is studied in the presence of 6-methyl-2-thouracil (3b) and 6-propyl-2-thiouracil (3a) as nucleophiles in a phosphate buffer (0.15 mol L −1 , pH = 6.8)/DMF (95:5) solution using cyclic voltammetry and controlled-potential coulometry. The results obtained indicate that the quinones derived from the catechols participate in 1,4-Michael-addition reactions with the nucleophiles to form the corresponding new benzothiazole compounds. In this work, we derive a variety of products with good yields using controlled potential at graphite electrodes in an undivided cell.

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Electrochemical studies of adrenergic neurotrans-mitters and related compounds

Cited by 169 publications

References 12 publications

Linking Adhesive and Structural Proteins in the Attachment Plaque of Mytilus californianus

Linking Adhesive and Structural Proteins in the Attachment Plaque of Mytilus californianus

The Electrochemical Oxidation of Substituted Catechols

Clean and Green Synthesis of New Benzothiazole Derivatives via Electrochemical Oxidation of Catechol Derivatives

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