Spectroscopic and kinetic properties of the molybdenum-containing, NAD+-dependent formate dehydrogenase from Ralstonia eutropha

Journal of Biological Chemistry

Volumn 291, Issue 3, 2016, Pages 1162-1174

  Niks, Dimitri ^a   Duvvuru, Jayant ^a   Escalona, Miguel ^a   Hille, Russ ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; ELECTRON RESONANCE; ENZYMES; IRON; KINETICS; MAGNETIC RESONANCE; PARAMAGNETIC RESONANCE; PARAMAGNETISM; REACTION KINETICS;

ENZYME REDUCTIONS; FORMATE DEHYDROGENASE; KINETIC PROPERTIES; MAGNETIC INTERACTIONS; RALSTONIA EUTROPHA; REACTION MECHANISM; SPECTROSCOPIC PROPERTY; VARYING TEMPERATURE;

MOLYBDENUM;

FORMATE DEHYDROGENASE; MOLYBDENUM; NAD DEPENDENT FDSABG FORMATE DEHYDROGENASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; FLAVINE MONONUCLEOTIDE; FORMIC ACID; FORMIC ACID DERIVATIVE; IRON SULFUR PROTEIN; METALLOPROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN SUBUNIT;

ARTICLE; CHEMICAL PHENOMENA; CONTROLLED STUDY; CUPRIAVIDUS NECATOR; DIRECT HYDRIDE TRANSFER; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME SPECTROSCOPY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; MAGNETISM; MOLECULAR MODEL; MOLYBDENUM CENTER; NONHUMAN; PRIORITY JOURNAL; SIMULATION; SPECTROSCOPY; STEADY STATE; STRUCTURE ACTIVITY RELATION; TEMPERATURE DEPENDENCE; ULTRAVIOLET SPECTROSCOPY; BIOCATALYSIS; CHEMISTRY; COLD; ENZYMOLOGY; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; OXIDATION REDUCTION REACTION; PH; PROTEIN CONFORMATION; PROTEIN SUBUNIT; SPECTROPHOTOMETRY;

BACTERIAL PROTEINS; BIOCATALYSIS; COLD TEMPERATURE; CUPRIAVIDUS NECATOR; ELECTRON SPIN RESONANCE SPECTROSCOPY; FLAVIN MONONUCLEOTIDE; FORMATE DEHYDROGENASES; FORMATES; HYDROGEN-ION CONCENTRATION; IRON-SULFUR PROTEINS; KINETICS; METALLOPROTEINS; MODELS, MOLECULAR; MOLYBDENUM; NAD; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SPECTROPHOTOMETRY;

EID: 84954481803     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.688457     Document Type: Article

References (33)

1. Hille, R., Hall, J., and Basu, P. (2014) The mononuclear molybdenum enzymes. Chem. Rev. 114, 3963-4038
2. Sazanov, L. A., and Hinchliffe, P. (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311, 1430-1436
3. Efremov, R. G., Baradaran, R., and Sazanov, L. A. (2010) The architecture of respiratory complex I. Nature 465, 441-445
4. +-linked formate dehydrogenase of Ralstonia eutropha. J. Biol. Chem. 273, 26349-26360
5. Boyington, J. C., Gladyshev, V. N., Khangulov, S. V., Stadtman, T. C., and Sun, P. D. (1997) Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science 275, 1305-1308
6. Rothery, R. A., Workun, G. J., and Weiner, J. H. (2008) The prokaryotic complex iron-sulfur molybdoenzyme family. Biochim. Biophys. Acta 1778, 1897-1929
7. Hille R. (1996) The mononuclear molybdenum enzymes. Chem. Rev 96, 2757-2816
8. Thomé, R., Gust, A., Toci, R., Mendel, R., Bittner, F., Magalon, A., and Walburger, A. (2012)Asulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli. J. Biol. Chem. 287, 4671-4678
9. Schrapers, P., Hartmann, T., Kositzki, R., Dau, H., Reschke, S., Schulzke, C., Leimkühler, S., and Haumann, M. (2015) Sulfido and cysteine ligation changes at the molybdenum cofactor during substrate conversion by formate dehydrogenase (FDH) from Rhodobacter capsulatus. Inorg. Chem. 54, 3260-3271
10. Friedebold, J., and Bowien, B. (1993) Physiological and biochemical characterization of the soluble formate dehydrogenase, a molybdoenzyme from Alcaligenes eutrophus. J. Bacteriol. 175, 4719-4728
11. Friedebold, J., Mayer, F., Bill, E., Trautwein, A. X., and Bowien, B. (1995) Structural and immunological studies on the soluble formate dehydrogenase from Alcaligenes eutrophus. Biol. Chem. Hoppe-Seyler 376, 561-568
12. Stoll, S., and Schweiger, A. (2006) Easy Spin, a comprehensive software package for spectral simulation and analysis in EPR. J. Magn. Reson. 178, 42-55
13. Olson, J. S., Ballou, D. P., Palmer, G., and Massey, V. (1974) Mechanism of action of xanthine oxidase. J. Biol. Chem. 249, 4363-4382
14. Edmondson, D., Ballou, D., Van Heuvelen, A., Palmer, G., and Massey V. (1973) Kinetic studies on substrate reduction of xanthine oxidase. J. Biol. Chem. 248, 6135-6144
15. Brody, M. S., and Hille, R. (1999) The kinetic behavior of chicken liver sulfite oxidase. Biochemistry 38, 6668-6677
16. 2 to formate. FEBS J. 280, 6083-6096
17. Bennett, B., Benson, N., McEwan, A. G., and Bray, R. C. (1994) Multiple states of the molybdenum center of dimethylsulfoxide reductase from Rhodobacter capsulatus revealed by EPR. Eur. J. Biochem. 225, 321-331
18. Bray, R. C., Knowles, P. F., Pick, F. M., and Vänngård, T. (1968) Electron spin resonance evidence for interaction of protons with Mo(V) in reduced froms of xanthine oxidase. Biochem. J. 107, 601-602
19. Bray, R. C., and Vänngård, T. (1969) "Rapidly appearing" molybdenum electron paramagnetic resonance signals from xanthine oxidase. Biochem. J. 114, 725-734
20. Hille, R. (1994) The reaction mechanism of oxomolybdenum enzymes. Biochim. Biophys. Acta 1184, 143-169
21. Huber, R., Hof, P., Duarte, R. O., Moura, J. J., Moura, I., Liu, M.-Y., LeGall, J., Hille, R., Archer, M., and Romão, M. J. (1996) A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes. Proc. Natl. Acad. Sci. U.S.A. 93, 8846-8851
22. Xia, M., Dempski, R., and Hille R. (1999) The reductive half-reaction of xanthine oxidase: reaction with aldehyde substrates and identification of the catalytically labile oxygen. J. Biol. Chem. 274, 3323-3330
23. Gutteridge, S., Tanner, S. J., and Bray R. C. (1978) The molybdenum center of xanthine oxidase: evidence for proton transfer from substrates to the center and for the existence of an anion binding site. Biochem. J. 175, 869-878
24. Gutteridge, S., Tanner, S. J., and Bray, R. C. (1978) Comparison of the molybdenum centers of native and desulfo xanthine oxidase: nature of the cyanide-labile sulfur atom and nature of the proton-accepting group. Biochem. J. 175, 887-897
25. Malthouse, J. P., Gutteridge, S., and Bray, R. C. (1980) Rapid type-2 molybdenum(V) electron paramagnetic resonance signals from xanthine oxidase and the structure of the active center of the enzyme. Biochem. J. 185, 767-770
26. Gutteridge, S., Bray, R. C. (1980) O-17 splitting of the very rapid molybdneum(V) electron paramagnetic resonance signal from xanthine oxidase: rate of exchange with water of the coupled oxygen. Biochem. J. 189, 615-623
27. Khangulov, S. V., Gladyshev, V. N., Dismukes, G. C., and Stadtman, T. C. (1998) Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer. Biochemistry 37, 3518-3528
28. Bordwell, F. G., Bartmess, J. E., and Hautala, J. A. (1978) Alkyl effects on equilibrium acidities of carbon acids in protic and dipolar aprotic media and the gas phase. J. Org. Chem. 43, 3113-3116
29. George, G. N., Colangelo, C. M., Dong, J., Scott, R. A., Khangulov, S. V., Gladyshev, V. N., and Stadtman, T. C. (1998) X-ray absorption spectroscopy of the molybdenum site of Escherichia coli formate dehydrogenase. J. Am. Chem. Soc. 120, 1267-1273
30. George, G. N., Costa, C., Moura. J. J. G., and Moura, I. (1999) Observation of ligand-based redox chemistry at the active site of a molybdenum enzyme. J. Am. Chem. Soc. 121, 2625-2626
31. McWhirter, R. B., and Hille, R. (1991) The reductive half-reaction of xanthine oxidase: identification of spectral intermediates in the hydroxylation of 2-hydroxy-6-methylpurine. J. Biol. Chem. 266, 23724-23731
32. V electronparamagnetic resonance signal. Biochemistry 32, 3973-39780
33. Finel, M. (1998) Organization and evolution of structural elements within complex I. Biochim. Biophys. Acta 1364, 112-121