Chloroacetaldehyde as a Sulfhydryl Reagent: The Role of Critical Thiol Groups in Ifosfamide Nephropathy

2006 ◽  
Vol 29 (5) ◽  
pp. 280-293 ◽  
Author(s):  
Andreas Benesic ◽  
Gerald Schwerdt ◽  
Ruth Freudinger ◽  
Sigrid Mildenberger ◽  
Franziska Groezinger ◽  
...  
Keyword(s):  
Thiol Groups ◽  
Sulfhydryl Reagent

scholarly journals Mechanism of porphobilinogen synthase. Possible role of essential thiol groups.

1977 ◽  
Vol 252 (24) ◽  
pp. 8965-8974 ◽  
Author(s):  
G.F. Barnard ◽  
R. Itoh ◽  
L.H. Hohberger ◽  
D. Shemin
Keyword(s):  
Thiol Groups ◽  
Porphobilinogen Synthase

On the molecular basis of pyruvate kinase deficiency II. Role of thiol groups in pyruvate kinase from pyruvate kinase-deficient patients

1974 ◽  
Vol 334 (2) ◽  
pp. 361-367 ◽  
Author(s):  
Th.J.C. Van Berkel ◽  
G.E.J. Staal ◽  
J.F. Koster ◽  
J.G. Nyessen ◽  
L. van Milligen-Boersma
Keyword(s):  
Pyruvate Kinase ◽  
Molecular Basis ◽  
Thiol Groups ◽  
Pyruvate Kinase Deficiency

scholarly journals Oxidation of human haemoglobin by copper. Mechanism and suggested role of the thiol group of residue β-93

1977 ◽  
Vol 165 (1) ◽  
pp. 141-148 ◽  
Author(s):  
C C Winterbourn ◽  
R W Carrell
Keyword(s):  
Electron Transfer ◽  
Binding Sites ◽  
Equilibrium Dialysis ◽  
Thiol Group ◽  
Thiol Groups ◽  
Human Haemoglobin ◽  
High Affinity ◽  
Rate Determining Step ◽  
Haemoglobin Molecule

Addition of Cu(II) ions to human oxyhaemoglobin caused the rapid oxidation of the haem groups of the beta-chain. Oxidation required binding of Cu(II) to sites involving the thiol group of beta-93 residues and was prevented when these groups were blocked with iodoacetamide or N-ethylmaleimide. Equilibrium-dialysis studies showed three pairs of binding sites, two pairs with high affinity for Cu(II) and one pair with lower affinity. It was the second pair of high-affinity sites that were blocked with iodoacetamide and were involved in haem oxidation. Cu(II) oxidized deoxyhaemoglobin at least ten times as fast as oxyhaemoglobin, and analysis of rates suggested that binding rather than electron transfer was the rate-determining step. No thiol-group oxidation to disulphides occurred during the period of haem oxidation, although it did occur subsequently in the presence of oxygen, or when Cu(II) was added to methaemoglobin. It is proposed that thiol oxidation did not occur because there exists a pathway of electron transfer between the haem group and copper bound to the beta-93 thiol groups. The route for this electron transfer is discussed, as well as the implications as to the function of the beta-93 cysteine in the haemoglobin molecule.

scholarly journals The Role of Xanthine Oxidase in Hemodialysis-Induced Oxidative Injury: Relationship with Nutritional Status

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Dijana Miric ◽  
Bojana Kisic ◽  
Radojica Stolic ◽  
Bratislav Miric ◽  
Radoslav Mitic ◽  
...  
Keyword(s):  
Xanthine Oxidase ◽  
Risk Index ◽  
Oxidative Injury ◽  
Chronic Hemodialysis ◽  
Nutritional Risk ◽  
Lipid Hydroperoxides ◽  
Thiol Groups ◽  
Nutritional Risk Index ◽  
Baseline Values

The role of xanthine oxidase (XOD) in patients undergoing chronic hemodialysis treatment (HD) is poorly understood. Geriatric nutritional risk index (GNRI) ≤ 90 could be linked with malnutrition-inflammation complex syndrome. This study measured XOD, myeloperoxidase (MPO), superoxide dismutase (SOD), lipid hydroperoxides, total free thiol groups, and advanced oxidation protein products (AOPP) in 50 HD patients before commencing (pre-HD) and immediately after completion of HD session (post-HD) and in 22 healthy controls. Pre-HD serum hydroperoxides, AOPP, XOD, and SOD were higher and total thiol groups were lower in patients than in controls (P<0.05, resp.). Compared to baseline values, serum MPO activity was increased irrespective of GNRI status. Serum XOD activity was increasing during HD treatment in the group with GNRI ≤ 90 (P=0.030) whilst decreasing in the group with GNRI > 90 (P=0.002). In a multiple regression analysis, post-HD serum XOD activity was independently associated with GNRI ≤ 90 (β  ± SE: 0.398 ± 0.151;P=0.012) and HD vintage (β  ± SE: −0.349 ± 0.139;P=0.016). These results indicate that an upregulated XOD may be implicated in HD-induced oxidative injury contributing to accelerated protein damage in patients with GNRI ≤ 90.

Role of Thiol Groups in Mn2+Dependent Guanidinoacetate Amidinohydrolase

1978 ◽  
Vol 42 (6) ◽  
pp. 1295-1296
Author(s):  
Hiroko Tamai ◽  
Hideki Usami ◽  
Takamitsu Yorifuji
Keyword(s):  
Thiol Groups

scholarly journals Low-Molecular-Weight Thiols and Thioredoxins Are Important Players in Hg(II) Resistance in Thermus thermophilus HB27

2017 ◽  
Vol 84 (2) ◽  
Author(s):  
J. Norambuena ◽  
Y. Wang ◽  
T. Hanson ◽  
J. M. Boyd ◽  
T. Barkay
Keyword(s):  
Heavy Metals ◽  
Molecular Weight ◽  
Thermus Thermophilus ◽  
Mercury Resistance ◽  
Low Molecular Weight ◽  
Thiol Groups ◽  
Content Type ◽  
Protein Thiols ◽  
Thioredoxin System

ABSTRACTMercury (Hg), one of the most toxic and widely distributed heavy metals, has a high affinity for thiol groups. Thiol groups reduce and sequester Hg. Therefore, low-molecular-weight (LMW) and protein thiols may be important cell components used in Hg resistance. To date, the role of low-molecular-weight thiols in Hg detoxification remains understudied. The mercury resistance (mer) operon ofThermus thermophilussuggests an evolutionary link between Hg(II) resistance and low-molecular-weight thiol metabolism. Themeroperon encodes an enzyme involved in methionine biosynthesis, Oah. Challenge with Hg(II) resulted in increased expression of genes involved in the biosynthesis of multiple low-molecular-weight thiols (cysteine, homocysteine, and bacillithiol), as well as the thioredoxin system. Phenotypic analysis of gene replacement mutants indicated that Oah contributes to Hg resistance under sulfur-limiting conditions, and strains lacking bacillithiol and/or thioredoxins are more sensitive to Hg(II) than the wild type. Growth in the presence of either a thiol-oxidizing agent or a thiol-alkylating agent increased sensitivity to Hg(II). Furthermore, exposure to 3 μM Hg(II) consumed all intracellular reduced bacillithiol and cysteine. Database searches indicate thatoah2is present in allThermussp.meroperons. The presence of a thiol-related gene was also detected in some alphaproteobacterialmeroperons, in which a glutathione reductase gene was present, supporting the role of thiols in Hg(II) detoxification. These results have led to a working model in which LMW thiols act as Hg(II)-buffering agents while Hg is reduced by MerA.IMPORTANCEThe survival of microorganisms in the presence of toxic metals is central to life's sustainability. The affinity of thiol groups for toxic heavy metals drives microbe-metal interactions and modulates metal toxicity. Mercury detoxification (mer) genes likely originated early in microbial evolution in geothermal environments. Little is known about howmersystems interact with cellular thiol systems.Thermusspp. possess a simplemeroperon in which a low-molecular-weight thiol biosynthesis gene is present, along withmerRandmerA. In this study, we present experimental evidence for the role of thiol systems in mercury resistance. Our data suggest that, inT. thermophilus, thiolated compounds may function side by side withmergenes to detoxify mercury. Thus, thiol systems function in consort withmer-mediated resistance to mercury, suggesting exciting new questions for future research.

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