Reversible inactivation of CO dehydrogenase with thiol compounds

Biochemical and Biophysical Research Communications

Volumn 447, Issue 3, 2014, Pages 413-418

  Kreß, Oliver ^a   Gnida, Manuel ^b   Pelzmann, Astrid M ^a   Marx, Christian ^c   Meyer Klaucke, Wolfram ^b   Meyer, Ortwin ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b UNIVERSITY OF PADERBORN   (Germany)

^c FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

Carbon monoxide dehydrogenase regulation; Copper; Molybdenum; Oligotropha carboxidovorans; Thiol; X ray absorption spectroscopy

Indexed keywords

ACETYLCYSTEINE; CARBON MONOXIDE DEHYDROGENASE; COENZYME A; CYSTEINE; CYSTEINEGLYCINE; DITHIOTHREITOL; HOMOCYSTEINE; MERCAPTOETHANOL; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME REGULATION; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; X RAY ABSORPTION SPECTROSCOPY;

CARBON MONOXIDE DEHYDROGENASE REGULATION; COPPER; MOLYBDENUM; OLIGOTROPHA CARBOXIDOVORANS; THIOL; X-RAY ABSORPTION SPECTROSCOPY;

ALDEHYDE OXIDOREDUCTASES; BACTERIAL PROTEINS; BRADYRHIZOBIACEAE; CATALYTIC DOMAIN; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; MOLYBDENUM; MULTIENZYME COMPLEXES; OXIDATION-REDUCTION; SULFHYDRYL COMPOUNDS;

EID: 84899936753     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.03.147     Document Type: Article

References (25)

1. Meyer O. Genus VII Oligotropha. Bergey's Manual of Systematic Bacteriology 2005, vol. 2:468-471. Springer, New York.
2. Dobbek H., Gremer L., Kiefersauer R., et al. Catalysis at a dinuclear [CuSMo(O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:15971-15976.
3. Meyer O., Schlegel H.G. Oxidation of carbon monoxide in cell extracts of Pseudomonas carboxydovorans. J. Bacteriol. 1979, 137:811-817.
4. Dobbek H., Gremer L., Meyer O., et al. Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:8884-8889.
5. Gremer L., Kellner S., Dobbek H., et al. Binding of a flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. J. Biol. Chem. 2000, 275:1864-1872.
6. Enroth C., Eger B.T., Okamoto K., et al. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:10723-10728.
7. Della Corte E., Stirpe F. The regulation of rat liver xanthine oxidase. Biochem. J. 1972, 126:739-745.
8. Battelli M.G., Lorenzoni E., Stirpe F. Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Biochem. J. 1973, 131:191-198.
9. Hille R. Structure and function of mononuclear molybdenum enzymes. J. Biol. Inorg. Chem. 1996, 1:397-404.
10. Mura U., Cappiello M., Vilardo P.G., et al. Signalling potential and protein modifying ability of physiological thiols. BioFactors 2003, 17:279-285.
11. Ziegler D.M. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu. Rev. Biochem. 1985, 54:305-329.
12. Maisel T., Joseph S., Mielke T., et al. The CoxD protein, a novel AAA+ ATPase involved in metal cluster assembly: hydrolysis of nucleotide triphosphates and oligomerization. PLoS ONE 2012, 7:e47424.
13. Meyer O. Chemical and spectral properties of carbon monoxide: methylene blue oxidoreductase. J. Biol. Chem. 1982, 257:1333-1341.
14. Kraut M., Hugendieck I., Herwig S., et al. Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria. Arch. Microbiol. 1989, 152:335-341.
15. Ravel B., Newville M. ATHENA, ARTEMIS, HEPHAESTUS: data analysis for X-ray absorption spectroscopy using IFEFFIT. J. Synchrotron Radiat. 2005, 12:537-541.
16. Binsted N., Strange R.W., Hasnain S.S. Constrained and restrained refinement in EXAFS data analysis with curved wave theory. Biochemistry 1992, 31:12117-12125.
17. Gnida M., Ferner R., Gremer L., et al. A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy. Biochemistry 2003, 42:222-230.
18. Kau L., Spira-Solomon D.J., Penner-Hahn J.E., et al. X-ray absorption edge determination of the oxidation state and coordination number of copper. Application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen. J. Am. Chem. Soc. 1987, 109:6433-6442.
19. Kutzler F.W., Natoli C.R., Misemer D.K., et al. Use of one-electron theory for the interpretation of near edge structure in K-shell X-ray absorption spectra of transition metal complexes. J. Chem. Phys. 1980, 73:3274-3288.
20. Pickering I.J., George G.N., Dameron C.T., et al. X-ray absorption spectroscopy of cuprous-thiolate clusters in proteins and model systems. J. Am. Chem. Soc. 1993, 115:9498-9505.
21. Siegbahn P.E.M., Shestakov A.F. Quantum chemical modeling of CO oxidation by the active site of molybdenum CO dehydrogenase. J. Comput. Chem. 2005, 26:888-898.
22. Hofmann M., Kassube J.K., Graf T. The mechanism of Mo-Cu-dependent CO dehydrogenase. J. Biol. Inorg. Chem. 2005, 10:490-495.
23. Kessler D. Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes. FEMS Microbiol. Rev. 2006, 30:825-840.
24. Vallari D.S., Jackowski S., Rock C.O. Regulation of pantothenate kinase by coenzyme A and its thioesters. J. Biol. Chem. 1987, 262:2468-2471.
25. 2] cluster. J. Biol. Chem. 2009, 284:9578-9586.