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Chemical Compound Review

Hydride     hydrogen(-1) anion

Synonyms: hydrogen anion, CHEBI:29239, AC1L4YHB, H(-), 12184-88-2
 
 
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Disease relevance of hydrogen anion

  • Accumulation of 10B in the central degenerative areas of human glioma and colon carcinoma spheroids after sulfhydryl boron hydride administration [1].
  • In a transplantable Harding-Passey melanoma in mice, it was found that the sulfhydryl boron hydride Na2B12H11SH presently used for therapy of glioblastoma clears blood, muscle, and brain very rapidly [2].
  • 6. A comparison of the ternary complexes in R67 and E. coli DHFRs suggests that enzymic raising of the pK(a) at N5 can significantly increase the catalytic efficiency of the hydride transfer step [3].
  • The mechanism for fumarate reduction by the soluble fumarate reductase from Shewanella frigidimarina involves hydride transfer from FAD and proton transfer from the active-site acid, Arg-402 [4].
  • Rates of hydride transfer at pH 7.65 cover a wide range, from 7 s-1 for DHFR from a strain of Lactobacillus casei (LCDHFR1) to 3000 s-1 for recombinant human DHFR (rHDHFR) [5].
 

Psychiatry related information on hydrogen anion

  • For examination of the possibility of an NAD+-mediated intramolecular hydride transfer of the 4'-hydrogen to a position on the side chain of oxoimidazolepropionate, the origins of hydrogen at positions 2 and 3 in the propionate chain were studied as a function of reaction time and extent of exchange of the 4'-hydrogen [6].
  • Hydride reduction of the amide carbonyl in 1 also yielded compounds having a slightly lower ED50 against convulsions induced by electroshock and a much lower TD50 in the rotorod assay [7].
  • Neuropsychological tests and self-report personality inventories were administered to 14 workers and rescue squad personnel approximately 2 months following mild exposure to pentaborane, a highly toxic volatile liquid boron hydride [8].
 

High impact information on hydrogen anion

  • Such tunnelling also allows sequential electron transfer in catalytic sites to surmount radical transition states without involving the movement of hydride ions, as is generally assumed [9].
  • The proton-coupled electron transfer reaction catalyzed by soybean lipoxygenase and the hydride transfer reaction catalyzed by dihydrofolate reductase are discussed [10].
  • Low-valent ruthenium and iridium hydride complexes are highly useful redox Lewis acid and base catalysts [11].
  • Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase [12].
  • This active site geometry allows for catalysis of hydride equivalent transfer to the >C5=NH of PQQ(NH) by concerted Glu-171CO(2)(-) general-base removal of the H-OCH3 proton and Arg-324H+ general-acid proton transfer to the imine nitrogen [13].
 

Chemical compound and disease context of hydrogen anion

 

Biological context of hydrogen anion

  • The transient-state kinetics of hydride transfer catalyzed by mixtures of recombinant domains I and III were studied by stopped-flow spectrophotometry [19].
  • Our data suggest that the decarboxylase domain catalyzes both hydride abstraction (oxidation) from the C-4' position and the subsequent decarboxylation [20].
  • Thus, it can be concluded that it is only the structure of the substrates that prevails in forming a ternary complex enzyme-NAD-thiohemiacetal productive (or not) for hydride transfer in the acylation step [21].
  • In dI, the lifetime of Trp-72 phosphorescence was barely affected by protein dimerization, cofactor binding, complexation with the NADP(H)-binding component (dIII), or by the introduction of two amino acid substitutions at the hydride-transfer site [22].
  • It is suggested that the rigidity and structural invariance of the protein domain (dI.1) housing this Trp residue are important to the mechanism of transhydrogenase: movement of dI.1 affects the width of a cleft which, in turn, regulates the positioning of bound nucleotides ready for hydride transfer [22].
 

Anatomical context of hydrogen anion

  • However, very little isotope was recovered from the washed mitochondria, indicating the possibility of hydride ion translocation in the absence of nucleotide translocation [23].
  • We assessed baseline selenium levels in serum and in toenail specimens (reflecting long-term intake) and post-intervention selenium levels in serum, and in prostate and SV tissues using hydride generation atomic fluorescence spectroscopy [24].
  • Chinese hamster ovary and mouse hybridoma cells were treated with silica hydride after being photosensitized with singlet oxygen, hydroxyl/superoxide, and hydroxyl reactive oxygen species through the use of rose Bengal diacetate, malachite green, and N,N'-bis(2-hydroperoxy-2-methoxyethyl)-1,4,5,8-naphthaldiimide, respectively [25].
  • This simple, rapid, sensitive, reliable, and economical assay for bismuth in plasma, erythrocytes, and urine is based on atomic absorption spectrophotometry with hydride generation [26].
  • It is located in the inner mitochondrial membrane and catalyzes hydride ion transfer between NAD(H) and NADP(H) in a reaction that is coupled to proton translocation across the inner membrane [27].
 

Associations of hydrogen anion with other chemical compounds

  • In the absence of this binding site in QR2, the enzyme retains the essential catalytic machinery, including affinity for FAD, but cannot bind phosphorylated hydride donors [28].
  • The effect of the mutation is both to increase the dissociation rate of dihydrofolate and decrease the rate of hydride transfer thus changing the rate-limiting step in catalysis from product loss (leucine-54) to hydride transfer (glycine-54) [29].
  • The protonmotive force alters the affinity of the transhydrogenase for substrates, accelerates the rate of hydride ion transfer from NADH to NADP, and shifts the equilibrium of this reaction toward NADPH formation [30].
  • This enzyme couples hydride transfer between NAD(H) and NADP(H) to proton translocation across a membrane and is only active as a dimer [22].
  • The nicotinamide nucleotide transhydrogenases of mitochondria and bacteria are proton pumps that couple direct hydride ion transfer between NAD(H) and NADP(H) bound, respectively, to extramembranous domains I and III to proton translocation by the membrane-intercalated domain II [31].
 

Gene context of hydrogen anion

  • The truncated AR delta 303-315 displayed a NADPH/D isotope effect in kcat and an increased D(kcat/Km) value for DL-glyceraldehyde, suggesting that hydride transfer has become partially rate-limiting for the overall reaction [32].
  • These values suggest that a significant 15N kinetic isotope effect is not associated with hydride transfer for LADH and FDH [33].
  • The lack of a Mg(2+) ion effect on hydride transfer was further demonstrated with an E399Q mutant of ALDH1 whose rate-limiting step had been changed from NADH dissociation to hydride transfer [34].
  • Detailed studies of W676H CPR indicate that further reduction of the enzyme beyond the two electron level is prevented due to the slow release of NADP(+) from the active site following the first hydride transfer from NADPH, owing to the stability of a reduced enzyme-NADP(+) charge-transfer complex [35].
  • Mouse ADH2 follows an ordered bi-bi mechanism, and hydride transfer is rate-limiting for oxidation of benzyl alcohols catalyzed by the mutated and wild-type enzymes [36].
 

Analytical, diagnostic and therapeutic context of hydrogen anion

References

  1. Accumulation of 10B in the central degenerative areas of human glioma and colon carcinoma spheroids after sulfhydryl boron hydride administration. Pettersson, O.A., Carlsson, J., Grusell, E. Cancer Res. (1992) [Pubmed]
  2. Quantitative neutron capture radiography for studying the biodistribution of tumor-seeking boron-containing compounds. Gabel, D., Holstein, H., Larsson, B., Gille, L., Ericson, G., Sacker, D., Som, P., Fairchild, R.G. Cancer Res. (1987) [Pubmed]
  3. Vibrational structure of dihydrofolate bound to R67 dihydrofolate reductase. Deng, H., Callender, R., Howell, E. J. Biol. Chem. (2001) [Pubmed]
  4. A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina. Pankhurst, K.L., Mowat, C.G., Rothery, E.L., Hudson, J.M., Jones, A.K., Miles, C.S., Walkinshaw, M.D., Armstrong, F.A., Reid, G.A., Chapman, S.K. J. Biol. Chem. (2006) [Pubmed]
  5. Hydride transfer by dihydrofolate reductase. Causes and consequences of the wide range of rates exhibited by bacterial and vertebrate enzymes. Beard, W.A., Appleman, J.R., Delcamp, T.J., Freisheim, J.H., Blakley, R.L. J. Biol. Chem. (1989) [Pubmed]
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  7. Synthesis and anticonvulsant activity of analogues of 4-amino-N-(1-phenylethyl)benzamide. Clark, C.R., Davenport, T.W. J. Med. Chem. (1987) [Pubmed]
  8. Neuropsychological function following mild exposure to pentaborane. Hart, R.P., Silverman, J.J., Garrettson, L.K., Schulz, C., Hamer, R.M. Am. J. Ind. Med. (1984) [Pubmed]
  9. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Page, C.C., Moser, C.C., Chen, X., Dutton, P.L. Nature (1999) [Pubmed]
  10. Hydrogen tunneling and protein motion in enzyme reactions. Hammes-Schiffer, S. Acc. Chem. Res. (2006) [Pubmed]
  11. Low-valent ruthenium and iridium hydride complexes as alternatives to Lewis acid and base catalysts. Murahashi, S., Takaya, H. Acc. Chem. Res. (2000) [Pubmed]
  12. Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase. Wong, K.F., Selzer, T., Benkovic, S.J., Hammes-Schiffer, S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  13. Mechanisms of ammonia activation and ammonium ion inhibition of quinoprotein methanol dehydrogenase: a computational approach. Reddy, S.Y., Bruice, T.C. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  14. Hydride transfer reaction catalyzed by hyperthermophilic dihydrofolate reductase is dominated by quantum mechanical tunneling and is promoted by both inter- and intramonomeric correlated motions. Pang, J., Pu, J., Gao, J., Truhlar, D.G., Allemann, R.K. J. Am. Chem. Soc. (2006) [Pubmed]
  15. Analysis of hydride transfer and cofactor fluorescence decay in mutants of dihydrofolate reductase: possible evidence for participation of enzyme molecular motions in catalysis. Farnum, M.F., Magde, D., Howell, E.E., Hirai, J.T., Warren, M.S., Grimsley, J.K., Kraut, J. Biochemistry (1991) [Pubmed]
  16. Catalysis by entropic guidance from enzymes. Young, L., Post, C.B. Biochemistry (1996) [Pubmed]
  17. A quantum mechanics/molecular mechanics study of the catalytic mechanism of the thymidylate synthase. Kanaan, N., Martí, S., Moliner, V., Kohen, A. Biochemistry (2007) [Pubmed]
  18. Mechanism of hydride transfer during the reduction of 3-acetylpyridine adenine dinucleotide by NADH catalyzed by the pyridine nucleotide transhydrogenase of Escherichia coli. Bragg, P.D. FEBS Lett. (1996) [Pubmed]
  19. Evidence that the transfer of hydride ion equivalents between nucleotides by proton-translocating transhydrogenase is direct. Venning, J.D., Grimley, R.L., Bizouarn, T., Cotton, N.P., Jackson, J.B. J. Biol. Chem. (1997) [Pubmed]
  20. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. Williams, G.J., Breazeale, S.D., Raetz, C.R., Naismith, J.H. J. Biol. Chem. (2005) [Pubmed]
  21. Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase. Boschi-Muller, S., Azza, S., Pollastro, D., Corbier, C., Branlant, G. J. Biol. Chem. (1997) [Pubmed]
  22. Tryptophan phosphorescence spectroscopy reveals that a domain in the NAD(H)-binding component (dI) of transhydrogenase from Rhodospirillum rubrum has an extremely rigid and conformationally homogeneous protein core. Broos, J., Gabellieri, E., van Boxel, G.I., Jackson, J.B., Strambini, G.B. J. Biol. Chem. (2003) [Pubmed]
  23. Demonstration and possible function of NADH:NAD+ transhydrogenase from ascaris muscle mitochondria. Köhler, P., Saz, H.J. J. Biol. Chem. (1976) [Pubmed]
  24. Selenium accumulation in prostate tissue during a randomized, controlled short-term trial of l-selenomethionine: a Southwest Oncology Group Study. Sabichi, A.L., Lee, J.J., Taylor, R.J., Thompson, I.M., Miles, B.J., Tangen, C.M., Minasian, L.M., Pisters, L.L., Caton, J.R., Basler, J.W., Lerner, S.P., Menter, D.G., Marshall, J.R., Crawford, E.D., Lippman, S.M. Clin. Cancer Res. (2006) [Pubmed]
  25. Antioxidant capacity of silica hydride: a combinational photosensitization and fluorescence detection assay. Stephanson, C.J., Flanagan, G.P. Free Radic. Biol. Med. (2003) [Pubmed]
  26. Improved assay for bismuth in biological samples by atomic absorption spectrophotometry with hydride generation. Froomes, P.R., Wan, A.T., Harrison, P.M., McLean, A.J. Clin. Chem. (1988) [Pubmed]
  27. Mitochondrial nicotinamide nucleotide transhydrogenase: NADPH binding increases and NADP binding decreases the acidity and susceptibility to modification of cysteine-893. Yamaguchi, M., Hatefi, Y. Biochemistry (1989) [Pubmed]
  28. Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase). Zhao, Q., Yang, X.L., Holtzclaw, W.D., Talalay, P. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  29. Importance of a hydrophobic residue in binding and catalysis by dihydrofolate reductase. Mayer, R.J., Chen, J.T., Taira, K., Fierke, C.A., Benkovic, S.J. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  30. Nicotinamide nucleotide transhydrogenase: a model for utilization of substrate binding energy for proton translocation. Hatefi, Y., Yamaguchi, M. FASEB J. (1996) [Pubmed]
  31. The proton channel of the energy-transducing nicotinamide nucleotide transhydrogenase of Escherichia coli. Yamaguchi, M., Stout, C.D., Hatefi, Y. J. Biol. Chem. (2002) [Pubmed]
  32. Catalytic effectiveness of human aldose reductase. Critical role of C-terminal domain. Bohren, K.M., Grimshaw, C.E., Gabbay, K.H. J. Biol. Chem. (1992) [Pubmed]
  33. Secondary 15N isotope effects on the reactions catalyzed by alcohol and formate dehydrogenases. Rotberg, N.S., Cleland, W.W. Biochemistry (1991) [Pubmed]
  34. Differential effects of Mg2+ ions on the individual kinetic steps of human cytosolic and mitochondrial aldehyde dehydrogenases. Ho, K.K., Allali-Hassani, A., Hurley, T.D., Weiner, H. Biochemistry (2005) [Pubmed]
  35. Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: properties of the soluble W676H and W676A mutant reductases. Gutierrez, A., Doehr, O., Paine, M., Wolf, C.R., Scrutton, N.S., Roberts, G.C. Biochemistry (2000) [Pubmed]
  36. Enzymatic mechanism of low-activity mouse alcohol dehydrogenase 2. Strömberg, P., Svensson, S., Berst, K.B., Plapp, B.V., Höög, J.O. Biochemistry (2004) [Pubmed]
  37. Silylene hydride complexes of molybdenum with silicon-hydrogen interactions: neutron structure of (eta(5)-C(5)Me(5))(Me(2)PCH(2)CH(2)PMe(2))Mo(H)(SiEt(2)). Mork, B.V., Tilley, T.D., Schultz, A.J., Cowan, J.A. J. Am. Chem. Soc. (2004) [Pubmed]
  38. Short-column liquid chromatography with hydride generation atomic fluorescence detection for the speciation of arsenic. Le, X.C., Ma, M. Anal. Chem. (1998) [Pubmed]
  39. Determination of arsenobetaine, arsenocholine, and tetramethylarsonium cations by liquid chromatography-thermochemical hydride generation-atomic absorption spectrometry. Blais, J.S., Momplaisir, G.M., Marshall, W.D. Anal. Chem. (1990) [Pubmed]
 
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