An Adenosine Triphosphate-Phosphate Exchange Catalyzed by a Soluble Enzyme Couple Inhibited by Uncouplers of Oxidative Phosphorylation

Allison, William S.; Benitez, Lita V.

doi:10.1073/pnas.69.10.3004

Cited by 23 publications

(11 citation statements)

References 22 publications

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“…A considerable proportion of the soluble ATPase activity could thus be due to these 'nothing kinase' activities. A further possible source may be sulphenyl glyceraldehyde phosphate dehydrogenase, which undoubtedly was present, acting in the way described by Allison & Benitez (1972).…”

Section: Discussionmentioning

confidence: 98%

Studies with a reconstituted muscle glycolytic system. The rate and extent of glycolysis in simulated post-mortem conditions

Scopes¹

1974

Biochemical Journal

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The reconstituted glycolytic system described previously (Scopes, 1973) was used to simulate post-mortem glycolytic metabolism in muscle. The effects of the following factors have been investigated: ATPase (adenosine triphosphatase) amount, AMP deaminase amount, percentage of the phosphorylase in the a form and the effect of diluting the glycolytic enzyme complex as a whole. It was confirmed that the rate of metabolism was solely dependent on the amount of ATPase present and that various concentrations of the glycolytic enzymes had no effect over a wide range encompassing the variation found in anatomically different muscles. The extent of metabolism, represented by the value of the ;ultimate' pH, depended markedly on the amount of phosphorylase in the a form; as little as 1% of the a form resulted in a considerably lower pH than in its absence. To a lesser extent the amount of AMP deaminase also affected the ultimate pH, but this was probably only significant for comparisons of genetically distinct muscles with widely differing amounts of AMP deaminase. The reconstituted system behaved almost identically with regard to post-mortem glycolytic metabolism compared with intact muscle tissue. It is concluded that the controlling effectors found with the reconstituted system apply to intact muscle also.

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Section: Discussionmentioning

confidence: 98%

Studies with a reconstituted muscle glycolytic system. The rate and extent of glycolysis in simulated post-mortem conditions

Scopes¹

1974

Biochemical Journal

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“…The discovery that the specific conversion of Cys-149 in GAPDH to corresponding sulfenic acid converts the enzyme from dehydrogenase to an acyl phosphatase was probably the first to hint at a biological role for protein sulfenic acid [68,72,73]. Another study demonstrated oxidation of the lone free thiol in albumin upon incubation with xanthine oxidase [74].…”

Section: Sulfenic Acids In Proteinsmentioning

confidence: 99%

Sulfenic acid chemistry, detection and cellular lifetime

Gupta

Carroll

2014

Biochimica et Biophysica Acta (BBA) - General Subjects

377

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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“…However, there is evidence that some protein sulfenates are sufficiently stable to operate as post-translational regulators of function in some proteins. For example, it is established that a number of transcription factors form regulatory sulfenic acids, including OxyR, OhrR, and Yap1 (9, 12, 13, 28 -30) Other proteins that form sulfenates include members of the NAD(P)H:disulfide reductase family, tyrosine phosphatases, peroxidases, and methionine sulfoxide reductases However, most of these are bacterial proteins, although some mammalian proteins have been identified (14,(31)(32)(33).…”

Section: Fig 8 a Western Blot Obtained From Isolated Hearts That Hmentioning

confidence: 99%

Protein Sulfenation as a Redox Sensor

Charles

Schröder

May

et al. 2007

Molecular & Cellular Proteomics

176

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Protein sulfenic acids are reactive intermediates in the catalytic cycles of many enzymes as well as the in formation of other redox states. Sulfenic acid formation is a reversible post-translational modification with potential for protein regulation. Dimedone (5,5-dimethyl-1,3-cyclohexanedione) is commonly used in vitro to study sulfenation of purified proteins, selectively "tagging" them, allowing monitoring by mass spectrometry. However dimedone is of little use in complex protein mixtures because selective monitoring of labeling is not possible. To address this issue, we synthesized a novel biotinylated derivative of dimedone, keeping the dione cassette required for sulfenate reactivity but adding the functionality of a biotin tag. Biotin-amido(5-methyl-5-carboxamidocyclohexane 1,3-dione) tetragol (biotin dimedone) was prepared in six steps, combining 3,5-dimethoxybenzoic acid (Birch reduction, ultimately leading to the dimedone unit with a carboxylate functionality), 1-amino-11-azido-3,6,9-trioxaundecane (a differentially substituted tetragol spacer), and biotin. We loaded biotin dimedone (0.1 mM, 30 min) into rat ventricular myocytes, treated them with H 2 O 2 (0.1-10,000 M, 5 min), and monitored derivatization on Western blots using streptavidin-horseradish peroxidase. There was a dose-dependent increase in labeling of multiple proteins that was maximal at 0.1 or 1 mM H 2 O 2 and declined sharply below basal with 10 mM treatment. Cellwide labeling was observed in fixed cells probed with avidin-FITC using a confocal fluorescence microscope. Similar H 2 O 2 -induced labeling was observed in isolated rat hearts. Hearts loaded and subjected to hypoxia showed a striking loss of labeling, which returned when oxygen was resupplied, highlighting the protein sulfenates as oxygen sensors. Cardiac proteins that were sulfenated during oxidative stress were purified with avidin-agarose and identified by separation of tryptic digests by liquid chromatography with on-line analysis by mass spectrometry.

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An Adenosine Triphosphate-Phosphate Exchange Catalyzed by a Soluble Enzyme Couple Inhibited by Uncouplers of Oxidative Phosphorylation

Cited by 23 publications

References 22 publications

Studies with a reconstituted muscle glycolytic system. The rate and extent of glycolysis in simulated post-mortem conditions

Studies with a reconstituted muscle glycolytic system. The rate and extent of glycolysis in simulated post-mortem conditions

Sulfenic acid chemistry, detection and cellular lifetime

Protein Sulfenation as a Redox Sensor

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