ChemInform Abstract: Unexpectedly Stable Sulfenic Acid: 4,6‐Dimethoxy‐1,3,5‐triazine‐2‐ sulfenic Acid; Synthesis, Properties, Molecular and Crystal Structure.

Tripolt, Robert; Belaj, Ferdinand; Nachbaur, E.

doi:10.1002/chin.199401231

Cited by 4 publications

(5 citation statements)

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“…In particular, we have no knowledge of the spectral features of sulfenic acid or sulfenate in this region of the UV spectrum, but studies with several small molecules stabilizing sulfenic acids have previously reported absorbance features in this region of the spectrum. 43,44 Furthermore, with the significant conformational changes associated with disulfide bond formation in AhpC, the environment of various residues is shifted and could contribute to the observed absorbance changes at 240 nm.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Dissecting Peroxiredoxin Catalysis: Separating Binding, Peroxidation, and Resolution for a Bacterial AhpC

Parsonage

Nelson²,

Ferrer-Sueta

et al. 2015

Biochemistry

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Peroxiredoxins make up a ubiquitous family of cysteine-dependent peroxidases that reduce hydroperoxide or peroxynitrite substrates through formation of a cysteine sulfenic acid (R-SOH) at the active site. In the 2-Cys peroxiredoxins, a second (resolving) cysteine reacts with the sulfenic acid to form a disulfide bond. For all peroxiredoxins, structural rearrangements in the vicinity of the active site cysteine(s) are necessary to allow disulfide bond formation and subsequent reductive recycling. In this study, we evaluated the rate constants for individual steps in the catalytic cycle of Salmonella typhimurium AhpC. Conserved Trp residues situated close to both peroxidatic and resolving cysteines in AhpC give rise to large changes in fluorescence during the catalytic cycle. For recycling, AhpF very efficiently reduces the AhpC disulfide, with a single discernible step and a rate constant of 2.3 × 107 M−1 s−1. Peroxide reduction was more complex and could be modeled as three steps, beginning with a reversible binding of H2O2 to the enzyme (k1 = 1.36 × 108 M−1 s−1, and k−1 = 53 s−1), followed by rapid sulfenic acid generation (620 s−1) and then rate-limiting disulfide bond formation (75 s−1). Using bulkier hydroperoxide substrates with higher Km values, we found that different efficiencies (kcat/Km) for turnover of AhpC with these substrates are primarily caused by their slower rates of binding. Our findings indicate that this bacterial peroxiredoxin exhibits rates for both reducing and oxidizing parts of the catalytic cycle that are among the fastest observed so far for this diverse family of enzymes.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Dissecting Peroxiredoxin Catalysis: Separating Binding, Peroxidation, and Resolution for a Bacterial AhpC

Parsonage

Nelson²,

Ferrer-Sueta

et al. 2015

Biochemistry

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“…The oxidation of 4,6-dimethoxy-1,3,5-triazine-2(1H)-thione (38) with 2-benzenesulfonyl-3- p -nitrophenyloxaziridine in THF solution gave 4,6-dimethoxy-1,3,5-triazine-2-sulfenic acid (39) as a stable crystalline solid (Scheme 4, equation 5). According to their 13 C NMR and X-ray analysis, 39 adopts the sulfenyl structure in condensed phase but in the crystal, the molecules form dimers linked by two strong intermolecular hydrogen bonds [38]. In another interesting study on the synthesis of unnaturally configured cephalo-sporins from 6-phthalimidopenicillanates, Baldwin et al isolated an unusually stable azitidinone sulfenic acid (41) (Scheme 4, equation 6).…”

Section: The Chemistry Of Sulfenic Acidmentioning

confidence: 99%

Sulfenic acid chemistry, detection and cellular lifetime

Gupta

Carroll

2014

Biochimica et Biophysica Acta (BBA) - General Subjects

383

399

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Background Reactive oxygen species-mediated cysteine sulfenic acid modification has emerged as an important regulatory mechanism in cell signaling. The stability of sulfenic acid in proteins is dictated by the local microenvironment and ability of antioxidants to reduce this modification. Several techniques for detecting this cysteine modification have been developed, including direct and in situ methods. Scope of review This review presents a historical discussion of sulfenic acid chemistry and highlights key examples of this modification in proteins. A comprehensive survey of available detection techniques with advantages and limitations is discussed. Finally, issues pertaining to rates of sulfenic acid formation, reduction, and chemical trapping methods are also covered. Major conclusions Early chemical models of sulfenic acid yielded important insights into the unique reactivity of this species. Subsequent pioneering studies led to the characterization of sulfenic acid formation in proteins. In parallel, the discovery of oxidant-mediated cell signaling pathways and pathological oxidative stress has led to significant interest in methods to detect these modifications. Advanced methods allow for direct chemical trapping of protein sulfenic acids directly in cells and tissues. At the same time, many sulfenic acids are short-lived and the reactivity of current probes must be improved to sample these species, while at the same time, preserving their chemical selectivity. Inhibitors with binding scaffolds can be rationally designed to target sulfenic acid modifications in specific proteins. General significance Ever increasing roles for protein sulfenic acids have been uncovered in physiology and pathology. A more complete understanding of sulfenic acid-mediated regulatory mechanisms will continue to require rigorous and new chemical insights. This article is part of a Special Issue entitled Current methods to study reactive oxygen species - pros and cons and biophysics of membrane proteins. Guest Editor: Christine Winterbourn.

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“…In some cases, proteins containing sulfenic acids may exhibit a low extinction absorbance band (ε max of ∼320 to 370 nm) due to the presence of the deprotonated sulfenate species (Poole and Ellis, 2002), as has been observed previously in small molecules (Tripolt et al, 1993). In these cases, lowering of the pH to protonate this group will result in the disappearance of this absorbance band.…”

Section: Determination Of the Protein Sulfenic Acid Dissociation Consmentioning

confidence: 62%

Measurement of Protein Sulfenic Acid Content

Poole

2008

CP Toxicology

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Protein sulfenic acids are reactive, reversibly oxidized cysteinyl residues with roles in redox catalysis and regulation. Detection and quantification of these species in proteins is accomplished through chemical modification by reagents such as 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD chloride), 2-nitro-5-thiobenzoate (TNB), dimedone, or derivatives of dimedone, followed by UV-visible spectroscopy or mass spectrometric analysis.

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ChemInform Abstract: Unexpectedly Stable Sulfenic Acid: 4,6‐Dimethoxy‐1,3,5‐triazine‐2‐ sulfenic Acid; Synthesis, Properties, Molecular and Crystal Structure.

Cited by 4 publications

References 1 publication

Dissecting Peroxiredoxin Catalysis: Separating Binding, Peroxidation, and Resolution for a Bacterial AhpC

Dissecting Peroxiredoxin Catalysis: Separating Binding, Peroxidation, and Resolution for a Bacterial AhpC

Sulfenic acid chemistry, detection and cellular lifetime

Measurement of Protein Sulfenic Acid Content

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