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Molybdenum-Containing Enzymes

  • Dimitri Niks
  • Russ Hille
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1876)

Abstract

An overview of modern methods used in the preparation and characterization of molybdenum-containing enzymes is presented, with an emphasis on those methods that have been developed over the past decade to address specific difficulties frequently encountered in studies of these enzymes.

Key words

Molybdenum enzymes Xanthine oxidase Sulfite oxidase DMSO reductase Anaerobiosis 

Notes

Acknowledgments

Work in the authors’ laboratory is supported by a grant from the Department of Energy (DE-SC0010666 to RH).

References

  1. 1.
    Brewer PG (1975) Minor elements in seawater. In: Riley JP (ed) Chemical oceanography, vol 1. Academic Press, New York, pp 415–496Google Scholar
  2. 2.
    Collier RW (1985) Molybdenum in the northeast Pacific Ocean. Limnol Oceanogr 30:1351–1354CrossRefGoogle Scholar
  3. 3.
    Weiss MC, Sousa FL, Mrnjavac N et al (2016) The physiology and habitat of the last universal common ancestor. Nat Microbiol 1:16116CrossRefGoogle Scholar
  4. 4.
    Hille R, Hall J, Basu P (2014) The mononuclear molybdenum enzymes. Chem Rev 114:3963–4038CrossRefGoogle Scholar
  5. 5.
    Hille R (1996) The mononuclear enzymes. Chem Rev 96:2757–2816CrossRefGoogle Scholar
  6. 6.
    Dixon M, Thurlow S (1924) Studies on xanthine oxidase. I. Preparation and properties of the active material. Biochem J 18:971–975CrossRefGoogle Scholar
  7. 7.
    Massey V, Edmondson DE (1970) Mechanism of inactivation of xanthine oxidase by cyanide. J Biol Chem 245:6595–6598PubMedGoogle Scholar
  8. 8.
    Wahl RC, Rajagopalan KV (1982) Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases. J Biol Chem 257:1354–1359PubMedGoogle Scholar
  9. 9.
    Bergel F, Bray RC (1956) Stabilization of xanthine oxidase activity by salicylate. Nature 178:88–89CrossRefGoogle Scholar
  10. 10.
    Friedebold J, Bowien B (1993) Physiological and biochemical characterization of the soluble formate dehydrogenase, a molybdoenzyme from Alcaligenes eutrophus. J Bacteriol 175:4719–4728CrossRefGoogle Scholar
  11. 11.
    Resch M, Dobbek H, Meyer O (2005) Structural and functional reconstitution in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide-oxidizing eubacterium Oligotropha carboxidovorans. J Biol Inorg Chem 5:518–528CrossRefGoogle Scholar
  12. 12.
    Mee JF (2004) The role of micronutrients in bovine periparturient problems. Cattle Pract 12:95–108Google Scholar
  13. 13.
    Li H-K, Temple C, Rajagopalan KV et al (2000) The 1.3 Å crystal structure of Rhodobacter sphaeroides dimethyl sulfoxie reductase reveals two distinct molybdenum coordination environments. J Am Chem Soc 122:7673–7680CrossRefGoogle Scholar
  14. 14.
    Bray RC, Adams B, Smith AT et al (2000) Reversible dissociation of thiolate ligands from molybdenum in an enzyme of the dimethyl sulfoxide reductase family. Biochemistry 39:11258–11269CrossRefGoogle Scholar
  15. 15.
    Mtei RP, Lyashenko G, Stein B et al (2011) Spectroscopic and electronic structure studies of a dimethyl sulfoxide reductase catalytic intermediate: implications for electron- and atom-transfer reactivity. J Am Chem Soc 133:9762–9774CrossRefGoogle Scholar
  16. 16.
    Mendel RR (2013) The molybdenum cofactor. J Biol Chem 288:13165–13172CrossRefGoogle Scholar
  17. 17.
    Leimkühler S, Iobbi-Nivol C (2013) Molybdenum enzymes, their maturation and molybdenum cofactor biosyntehsis in Escherichia coli. Biochim Biophys Acta 1827:1086–1101CrossRefGoogle Scholar
  18. 18.
    Iobbi-Nivol C, Leim kühler S (2013) Bacterial molybdeoenzymes: old enzymes for new purposes. FEMS Microbiol Rev 40:1–18Google Scholar
  19. 19.
    Warelow TP, Oke M, Schoepp-Cothenet B et al (2013) The respiratory arsenite oxidase: structure and the role of residues surrounding the Rieske cluster. PLoS One 8:e72535CrossRefGoogle Scholar
  20. 20.
    Temple CA, Graf TN, Rajagopalan KV (2000) Optimization of expression of human sulfite oxidase and its molybdenum domain. Arch Biochem Biophys 383:281–287CrossRefGoogle Scholar
  21. 21.
    Palmer T, Santini C-L, Lobbi-Nivol C et al (1996) Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli. Mol Microbiol 20:875–884CrossRefGoogle Scholar
  22. 22.
    Hartmann T, Leimkühler S (2013) The oxygen-tolerant and NAD+-dependent formate dehydrogenase from Rhodobacter capsulatus is able to catalyze the reduction of CO2 to formate. FEBS J 280:6083–6096CrossRefGoogle Scholar
  23. 23.
    Sabaty M, Grosse S, Adryanczyk G et al (2013) Detrimental effect of the 6 His C-terminal tag on YedY enzymatic activity and influence of the TAT signal sequence on YedY synthesis. BMC Biochem 14:28CrossRefGoogle Scholar
  24. 24.
    Arnau J, Lauritzen C, Petersen GE et al (2006) Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr Purif 48:1–13CrossRefGoogle Scholar
  25. 25.
    Johnson JL, Rajagopalan KV (1984) The pterin component of the molybdenum cofactor – structural characterization of 2 fluorescent derivative. J Biol Chem 259:5414–5422PubMedGoogle Scholar
  26. 26.
    Schumann S, Terao M, Garattini E et al (2009) Site directed mutagenesis of amino acid residues at the active site of mouse aldehyde oxidase AOX1. PLoS One 4:e5348CrossRefGoogle Scholar
  27. 27.
    Hille R (2010) EPR studies of xanthine oxidoreductase and other molybdenum-containing hydroxylases. In: Hanson G, Berliner L (eds) Metals in biology: applications of high-resolution EPR to metalloenzymes, Biological magnetic resonance, vol 29. Springer, Berlin, pp 91–120CrossRefGoogle Scholar
  28. 28.
    Kappler U, Schwarz G (2017) The sulfite oxidase family of molybdenum enzymes. In: Hille R, Schulzke C, Kirk ML (eds) Molybdenum and tungsten enzymes: biochemistry. RSC Press, London, pp 240–273Google Scholar
  29. 29.
    Beinert H, Orme-Johnson WH, Palmer G (1978) Special techniques for the preparation of samples for low-temperature EPR spectroscopy. Methods Enzymol 54:111–132CrossRefGoogle Scholar
  30. 30.
    Foust GP, Burleigh BD, Mayhew SG et al (1969) An anaerobic titration assembly for spectrophotometric use. Anal Biochem 27:530–535CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Dimitri Niks
    • 1
  • Russ Hille
    • 1
  1. 1.Department of BiochemistryUniversity of California, RiversideRiversideUSA

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