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Interrupting the hydrogen bond network at the active site of human manganese superoxide dismutase.

Ramilo CA, Leveque V, Guan Y, Lepock JR, Tainer JA, Nick HS, Silverman DN
J Biol Chem 274 27711-6 (1999)
Cited: 28 times
EuropePMC logo PMID: 10488113

Abstract

Histidine 30 in human manganese superoxide dismutase (MnSOD) is located at a site partially exposed to solvent with its side chain participating in a hydrogen-bonded network that includes the active-site residues Tyr(166) and Tyr(34) and extends to the manganese-bound solvent molecule. We have replaced His(30) with a series of amino acids and Tyr(166) with Phe in human MnSOD. The crystal structure of the mutant of MnSOD containing Asn(30) superimposed closely with the wild type, but the side chain of Asn(30) did not participate in the hydrogen-bonded network in the active site. The catalytic activity of a number of mutants with replacements at position 30 and for the mutant containing Phe(166) showed a 10-40-fold decrease in k(cat). This is the same magnitude of decrease in k(cat) obtained with the replacement of Tyr(34) by Phe, suggesting that interrupting the hydrogen-bonded active-site network at any of the sites of these three participants (His(30), Tyr(34), and Tyr(166)) leads to an equivalent decrease in k(cat) and probably less efficient proton transfer to product peroxide. The specific geometry of His(30) on the hydrogen bond network is essential for stability since the disparate mutations H30S, H30A, and H30Q reduce T(m) by similar amounts (10-16 degrees C) compared with wild type.

Reviews - 2gds mentioned but not cited (1)

  1. The structure-function relationships and physiological roles of MnSOD mutants. Bonetta Valentino R. Biosci Rep 42 BSR20220202 (2022)

Articles - 2gds mentioned but not cited (1)

  1. Manganese superoxide dismutase regulates a metabolic switch during the mammalian cell cycle. Sarsour EH, Kalen AL, Xiao Z, Veenstra TD, Chaudhuri L, Venkataraman S, Reigan P, Buettner GR, Goswami PC. Cancer Res 72 3807-3816 (2012)


Reviews citing this publication (4)

  1. Superoxide dismutases and superoxide reductases. Sheng Y, Abreu IA, Cabelli DE, Maroney MJ, Miller AF, Teixeira M, Valentine JS. Chem Rev 114 3854-3918 (2014)
  2. Manganese superoxide dismutase (Sod2) and redox-control of signaling events that drive metastasis. Hempel N, Carrico PM, Melendez JA. Anticancer Agents Med Chem 11 191-201 (2011)
  3. A Review of the Catalytic Mechanism of Human Manganese Superoxide Dismutase. Azadmanesh J, Borgstahl GEO. Antioxidants (Basel) 7 E25 (2018)
  4. Human Mn-superoxide dismutase inactivation by peroxynitrite: a paradigm of metal-catalyzed tyrosine nitration in vitro and in vivo. Demicheli V, Moreno DM, Radi R. Metallomics 10 679-695 (2018)

Articles citing this publication (22)

  1. Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis. Perry JJ, Hearn AS, Cabelli DE, Nick HS, Tainer JA, Silverman DN. Biochemistry 48 3417-3424 (2009)
  2. Potent anti-tumor effects of an active site mutant of human manganese-superoxide dismutase. Evolutionary conservation of product inhibition. Davis CA, Hearn AS, Fletcher B, Bickford J, Garcia JE, Leveque V, Melendez JA, Silverman DN, Zucali J, Agarwal A, Nick HS. J Biol Chem 279 12769-12776 (2004)
  3. The 2.0A resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase. Atzenhofer W, Regelsberger G, Jacob U, Peschek G, Furtmüller P, Huber R, Obinger C. J Mol Biol 321 479-489 (2002)
  4. Lessons from nature: unraveling biological CH bond activation. Stone KL, Borovik AS. Curr Opin Chem Biol 13 114-118 (2009)
  5. Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase. Grove LE, Xie J, Yikilmaz E, Miller AF, Brunold TC. Inorg Chem 47 3978-3992 (2008)
  6. Amino acid substitution at the dimeric interface of human manganese superoxide dismutase. Hearn AS, Fan L, Lepock JR, Luba JP, Greenleaf WB, Cabelli DE, Tainer JA, Nick HS, Silverman DN. J Biol Chem 279 5861-5866 (2004)
  7. The crystal structure of superoxide dismutase from Plasmodium falciparum. Boucher IW, Brzozowski AM, Brannigan JA, Schnick C, Smith DJ, Kyes SA, Wilkinson AJ. BMC Struct Biol 6 20 (2006)
  8. Complete sequencing and oxidative modification of manganese superoxide dismutase in medulloblastoma cells. John JPP, Pollak A, Lubec G. Electrophoresis 30 3006-3016 (2009)
  9. Mn/Fe superoxide dismutase interaction fingerprints and prediction of oligomerization and metal cofactor from sequence. Wintjens R, Gilis D, Rooman M. Proteins 70 1564-1577 (2008)
  10. Substrate-analog binding and electrostatic surfaces of human manganese superoxide dismutase. Azadmanesh J, Trickel SR, Borgstahl GEO. J Struct Biol 199 68-75 (2017)
  11. A New Mixed-Valence Mn(II)Mn(III) Compound With Catalase and Superoxide Dismutase Activities. Costa RO, Ferreira SS, Pereira CA, Harmer JR, Noble CJ, Schenk G, Franco RWA, Resende JALC, Comba P, Roberts AE, Fernandes C, Horn A. Front Chem 6 491 (2018)
  12. Ca(2+) rise within a narrow window of concentration prevents functional injury of mitochondria exposed to hypoxia/reoxygenation by increasing antioxidative defence. Schild L, Plumeyer F, Reiser G. FEBS J 272 5844-5852 (2005)
  13. Rescue of deleterious mutations by the compensatory Y30F mutation in ketosteroid isomerase. Cha HJ, Jang DS, Kim YG, Hong BH, Woo JS, Kim KT, Choi KY. Mol Cells 36 39-46 (2013)
  14. Tissue-specific expression and molecular modeling of cytosolic manganese superoxide dismutases from the white shrimp Litopenaeus vannamei. Gómez-Anduro GA, Sotelo-Mundo RR, Muhlia-Almazán A, Yepiz-Plascencia G. Dev Comp Immunol 31 783-789 (2007)
  15. 15N-NMR characterization of His residues in and around the active site of FeSOD. Miller AF, Yikilmaz E, Vathyam S. Biochim Biophys Acta 1804 275-284 (2010)
  16. Engineering and characterization of human manganese superoxide dismutase mutants with high activity and low product inhibition. Chockalingam K, Luba J, Nick HS, Silverman DN, Zhao H. FEBS J 273 4853-4861 (2006)
  17. Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals. Azadmanesh J, Trickel SR, Weiss KL, Coates L, Borgstahl GE. Acta Crystallogr F Struct Biol Commun 73 235-240 (2017)
  18. The role of the local environment of engineered Tyr to Trp substitutions for probing the denaturation mechanism of FIS. Muñiz VA, Srinivasan S, Boswell SA, Meinhold DW, Childs T, Osuna R, Colón W. Protein Sci 20 302-312 (2011)
  19. Probing the metal specificity mechanism of superoxide dismutase from human pathogen Clostridium difficile. Li W, Wang H, Chen Z, Ye Q, Tian Y, Xu X, Huang Z, Li P, Tan X. Chem Commun (Camb) 50 584-586 (2014)
  20. A computational study towards understanding the mechanism of phosphodiester cleavage by two mononuclear Zn(II) complexes. Dong H. Phys Chem Chem Phys 12 10434-10443 (2010)
  21. Structures of two superoxide dismutases from Bacillus anthracis reveal a novel active centre. Boucher IW, Kalliomaa AK, Levdikov VM, Blagova EV, Fogg MJ, Brannigan JA, Wilson KS, Wilkinson AJ. Acta Crystallogr Sect F Struct Biol Cryst Commun 61 621-624 (2005)
  22. Thermal stability effects of removing the type-2 copper ligand His306 at the interface of nitrite reductase subunits. Stirpe A, Sportelli L, Wijma H, Verbeet MP, Guzzi R. Eur Biophys J 36 805-813 (2007)


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