The Mechanism of Inactivation of Glyceraldehyde 3-Phosphate Dehydrogenase by Tetrathionate, o-Iodosobenzoate, and Iodine Monochloride

Parker, Donald J.; Allison, William S.

doi:10.1016/s0021-9258(19)78208-8

Cited by 131 publications

(18 citation statements)

References 30 publications

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“…The detection of 92% of I in the low M r fraction indicates that sulfenyl iodide, formed during the attack of trans , cis -[Pt(en)(OH) 2 I 2 ] on Cys34, is rapidly hydrolyzed to sulfenic acid. Our results are consistent with earlier studies, which reported that iodide is not incorporated into proteins after oxidation of cysteine by iodine/iodine monochloride, suggesting that sulfenyl iodide is hydrolyzed to sulfenic acid. , …”

Section: Discussionsupporting

confidence: 93%

“…These provide clues as to how such reactive intermediates might be stabilized in proteins. The reversible oxidation of cysteines in catalytic sites of proteins to sulfenic acids by second messengers, such as H 2 O 2 and NO, is important for the intracellular redox regulation of the activity of DNA binding domains of proteins, such as nuclear factor I (NFI),39g bovine papillomavirus,39a Fos, Jun,39h and OxyR transcription factors 39i and enzymes, such as NADH peroxidase,39c peroxiredoxins (Prx),39f papain and glyceraldehyde-3-phosphate dehydrogenase,39j alkyl hydroperoxide reductase,21b creatine kinase,33a and tyrosine phosphatases 21a. Criteria for the stabilization of Cys-SOH in proteins are 39c (1) the absence of other vicinal protein thiols, (2) limited solvent accessibility and association with apolar elements of the protein structure, (3) ionization to the conjugate sulfenate base, and (4) intramolecular hydrogen bonding.…”

Section: Discussionmentioning

confidence: 99%

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Surprising Reactions of Iodo Pt(IV) and Pt(II) Complexes with Human Albumin: Detection of Cys34 Sulfenic Acid

et al. 1999

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cis-[PtCl2(NH3)2] is the anticancer drug cisplatin, but the iodide analogue cis-[PtI2(NH3)2] is inactive. This inactivity is usually attributed to the greater stability and lower reactivity of Pt−I bonds compared to Pt−Cl in aqueous solution. Interest in reactions of Pt(IV) complexes with thiols arises from the reductive activation of Pt(IV) anticancer drugs in blood plasma. Recently, we found (J. Am. Chem. Soc. 1998, 120, 8253−8254) that low M r thiols react with Pt(IV)−I bonds of trans,cis-[Pt(en)(OH)2I2] via attack on the coordinated iodo ligand giving rise to reactive chelate-ring-opened Pt(II) ethylenediamine species. Here we report reactions of the Pt(II) and Pt(IV) complexes [Pt(en)I2] and trans,cis-[Pt(en)(OH)2I2] with the major thiol in blood plasma, Cys34 of the protein albumin (66 kDa). Unexpectedly, [Pt(en)I2] reacted more rapidly with albumin than the cisplatin analogue, [Pt(en)Cl2], and did not give products with Pt bound to Cys34. The Pt(IV) chloro analogue, trans,cis-[Pt(en)(OH)2Cl2], did not react at all with albumin. Reactions of trans,cis-[Pt(en)(OH)2I2] with the protein, via direct attack of an iodo ligand on Cys34, gave rise to a relatively stable sulfenic acid derivative, in contrast to reactions with low M r thiols. Reactions of Pt complexes with thiols in proteins can therefore take a different course: albumin can exert control over the reactivity of Cys34 and stabilize activated derivatives such as the sulfenyl iodide and sulfenic acid. The reactivity of iodide ligands in Pt complexes is much higher than has been previously recognized, and it may be possible to incorporate them into drug design strategies.

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Surprising Reactions of Iodo Pt(IV) and Pt(II) Complexes with Human Albumin: Detection of Cys34 Sulfenic Acid

et al. 1999

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“…In contrast to the results with the double-cysteine mutant, both channel-opening and -closing events were observed. Tetrathionate is known to modify single cysteines (Parker and Allison, 1969), and modification of the cysteine in the plug may have destabilized the closed state of the channel. Consistent with this assumption, channel opening was abolished by the addition of DTT.…”

Section: Resultsmentioning

confidence: 99%

Determining the Conductance of the SecY Protein Translocation Channel for Small Molecules

et al. 2007

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The channel formed by the SecY complex must maintain the membrane barrier for ions and other small molecules during the translocation of membrane or secretory proteins. We have tested the permeability of the channel by using planar bilayers containing reconstituted purified E. coli SecY complex. Wild-type SecY complex did not show any conductance for ions or water. Deletion of the "plug," a short helix normally located in the center of the SecY complex, or modification of a cysteine introduced into the plug resulted in transient channel openings; a similar effect was seen with a mutation in the pore ring, a constriction in the center of the channel. Permanent channel opening occurred when the plug was moved out of the way by disulfide-bridge formation. These data show that the resting channel on its own forms a barrier for small molecules, with both the pore ring and the plug required for the seal; channel opening requires movement of the plug.

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“…They concluded from their data that the active center sulfhydryl group (-SH) was not converted to a disulfide (S-S) but rather to a sulfenic acid (-SOH). On the basis of quite different experiments, Parker and Allison (1969) and Allison and Connors (1970) also reached the same conclusion and postulated further that the active enzyme-substrate complex might be an enzyme-sulfenylcarboxylate intermediate (ES0C(=0)CH3). Ehring and Colowick (1969) discovered a second phenomenon of importance.…”

Section: Discussionmentioning

confidence: 82%

Effects of photooxidation of histidine-38 on the acetylphosphatase activity of glyceraldehyde 3-phosphate dehydrogenase

Francis¹,

Meriwether²,

Park³

1973

Biochemistry

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The Mechanism of Inactivation of Glyceraldehyde 3-Phosphate Dehydrogenase by Tetrathionate, o-Iodosobenzoate, and Iodine Monochloride

Cited by 131 publications

References 30 publications

Surprising Reactions of Iodo Pt(IV) and Pt(II) Complexes with Human Albumin: Detection of Cys34 Sulfenic Acid

Surprising Reactions of Iodo Pt(IV) and Pt(II) Complexes with Human Albumin: Detection of Cys34 Sulfenic Acid

Determining the Conductance of the SecY Protein Translocation Channel for Small Molecules

Effects of photooxidation of histidine-38 on the acetylphosphatase activity of glyceraldehyde 3-phosphate dehydrogenase

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