The NADP-reducing hydrogenase from Desulfovibrio fructosovorans: Functional interaction between the C-terminal region of HndA and the N-terminal region of HndD subunits

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1556, Issue 2-3, 2002, Pages 217-225

  Dermoun, Zorah ^a,b   De Luca, Gilles ^a,b   Asso, Marcel ^a   Bertrand, Patrick ^a,b   Guerlesquin, Françoise ^a   Guigliarelli, Bruno ^a,b  

^a CNRS   (France)

^b AIX MARSEILLE UNIVERSITY   (France)

Author keywords

2Fe 2S domain; Desulfovibrio; Electron transfer; EPR; NADP reducing hydrogenase

Indexed keywords

FERROUS SULFATE; HYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN HNDA; PROTEIN HNDD; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DESULFOVIBRIO FRUCTOSOVORANS; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ESCHERICHIA COLI; MOLECULAR BIOLOGY; MOLECULAR CLONING; MOLECULAR INTERACTION; NONHUMAN; OXIDATION REDUCTION REACTION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; SPECTRUM;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DESULFOVIBRIO; ELECTRON SPIN RESONANCE SPECTROSCOPY; GENES, BACTERIAL; MOLECULAR SEQUENCE DATA; OPERON; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT;

DESULFOVIBRIO; DESULFOVIBRIO FRUCTOSOVORANS; ESCHERICHIA COLI;

EID: 0037010839     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(02)00364-X     Document Type: Article

References (38)

1. Stephenson M., Stickland L.H. Hydrogenase: a bacterial enzyme activating molecular hydrogen: I. The properties of the enzyme. Biochem. J. 25:1931;205-214.
2. Adams M.W.W., Mortenson L.E., Chen J.S. Hydrogenase. Biochim. Biophys. Acta. 594:1980;105-176.
3. 2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea. Eur. J. Biochem. 208:1992;511-520.
4. Buurman G., Shima S., Thauer R.K. The metal-free hydrogenase from methanogenic archaea: evidence for a bound cofactor. FEBS Lett. 485:2000;200-204.
5. Fauque G., Peck H.D. Jr., Moura J.J., Huynh B.H., Berlier Y., DerVartanian D.V., Teixeira M., Przybyla A.E., Lespinat P.A., Moura I., Legall J. The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio. FEMS Microbiol. Rev. 54:1988;299-344.
6. Albracht S.P. Nickel hydrogenases: in search of the active site. Biochim. Biophys. Acta. 1188:1994;167-204.
7. Volbeda A., Charon M.H., Piras C., Hatchikian E.C., Frey M., Fontecilla-Camps J.C. Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature. 373:1995;580-587.
8. Adams M.W.W. The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta. 1020:1990;115-145.
9. Vignais M.P., Billoud B., Meyer J. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25:2001;455-501.
10. Meyer J., Gagnon J. Primary structure of hydrogenase I from Clostridium pasteurianum. Biochemistry. 309:1991;3697-3704.
11. Verhagen M.J.M., O'Rourke T., Adams W.W.M. The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: amino acid sequence analyses versus biochemical characterization. Biochim. Biophys. Acta. 1412:1999;212-229.
12. Peters J.W., Lanzilotta W.N., Lemon B.J., Seefeldt L.C. X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science. 282:1998;1853-1858.
13. Nicolet Y., Piras C., Legrand P., Hatchikian C.E., Fontecilla-Camps J.C. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. Structure. 7:1999;13-23.
14. Pierik A.J., Hulstein W.R., Hagen W.R., Albracht S.P.J. A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases. Eur. J. Biochem. 258:1998;572-578.
15. Florin L., Tsokoglou A., Happe T. A novel type of iron hydrogenase in the green alga Scenedesmus obliquus is linked to the photosynthetic electron transport chain. J. Biol. Chem. 276:2001;6125-6132.
16. Kümmerle R., Kyritis P., Gaillard J., Moulis J.M. Electron transfer properties of iron-sulfur proteins. J. Inorg. Biochem. 79:2000;83-91.
17. Atta M., Lafferty M.E., Johnson M.K., Gaillard J., Meyer J. Heterologous biosynthesis and characterization of the [2Fe-2S]-containing N-terminal domain of Clostridium pasteurianum hydrogenase. Biochemistry. 37:1998;15974-15980.
18. Malki S., Saimmaime I., De Luca G., Rousset M., Dermoun Z., Bélaïch J.-P. Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J. Bacteriol. 177:1995;2628-2636.
19. De Luca G., Asso M., Bélaïch J.-P., Dermoun Z. Purification and characterization of the HndA subunit of NADP-reducing hydrogenase from Desulfovibrio fructosovorans overproduced in Escherichia coli. Biochemistry. 37:1998;2660-2665.
20. De Luca G., de Philip P., Rousset M., Bélaïch J.-P., Dermoun Z. The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity. Biochem. Biophys. Res. Commun. 248:1998;591-596.
21. Meyer J., Fujinaga J., Gaillard J., Lutz M. Mutated forms of the [2Fe-2S] ferredoxin from Clostridium pasteurianum with noncysteinyl ligands to the iron-sulfur cluster. Biochemistry. 33:1994;13642-13650.
22. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
23. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurements with the Folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
24. Bertrand P., Guigliarelli B., Gayda J.P., Setif P., Mathis P. An interpretation of the peculiar magnetic properties of center X in Photosystem I in terms of a 2Fe-2S cluster. Biochim. Biophys. Acta. 933:1988;393-397.
25. Cammack R. Iron-sulfur clusters in enzymes: themes and variations. Adv. Inorg. Chem. 38:1992;281-322.
26. Chatelet C., Gaillard J., Pétillot Y., Louwagie M., Meyer J. A [2Fe-2S] protein from the hyperthermophilic bacterium Aquifex aeolicus. Biochem. Biophys. Res. Commun. 261:1999;885-889.
27. Cardenas J., Mortenson L.E., Yoch D.C. Purification and properties of paramagnetic protein from Clostridium pasteurianum W5. Biochim. Biophys. Acta. 434:1976;244-257.
28. Crouse B.R., Yano T., Finnegan M.G., Yagi T., Johnson M.K. Properties of the iron-sulfur center in the 25-kilodalton subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. J. Biol. Chem. 269:1994;21030-21036.
29. Guigliarelli B., Bertrand P. Application of EPR spectroscopy to the structural and functional study of iron-sulfur proteins. Adv. Inorg. Chem. 47:1999;53-129.
30. Bertrand P., Gayda J.P. A theoretical interpretation of the variations of some physical parameters within the [2Fe-2S] ferredoxin group. Biochim. Biophys. Acta. 579:1979;107-121.
31. Bertrand P., Gayda J.P., Fee J.A., Kuila D., Cammack R. Comparison of the spin-lattice relaxation properties of the two classes of [2Fe-2S] clusters in proteins. Biochim. Biophys. Acta. 916:1987;24-28.
32. Chatelet C., Meyer J. The [2Fe-2S] protein I (Shetna protein I) from Azotobacter vinelandii is homologous to the [2Fe-2S] ferredoxin from Clostridium pasteurianum. J. Biol. Inorg Chem. 4:1999;311-317.
33. Verhagen F.J.M., O'Rourke T.W., Menon A.L., Adams M.W.W. Heterologous expression and properties of the γ-subunit of the Fe-only hydrogenase from Thermotoga maritima. Biochim. Biophys. Acta. 1505:2001;209-219.
34. Golinelli M.P., Chatelet C., Duin E., Johnson M.K., Meyer J. Extensive ligand rearrangements around the [2Fe-2S] cluster of Clostridium pasteurianum ferredoxin. Biochemistry. 37:1998;10429-10437.
35. Lloyd S.G., Franco R., Moura J.J.G., Moura I., Ferreira G.C., Huynh B.H. Functional necessity and physicochemical characteristics of the [2Fe-2S] cluster in mammalian ferrochelatase. J. Am. Chem. Soc. 118:1996;9892-9900.
36. Sellers V.M., Wang K.F., Johnson M.K., Dailey H.A. Evidence that the fourth ligand of the [2Fe-2S] cluster in animal ferrochelatase is a cysteine. J. Biol. Chem. 273:1998;22311-22316.
37. 1+ centers in molybdenum enzymes of the xanthine oxidase family: assignment of signals I and II. Biochemistry. 39:2000;2700-2707.
38. Werth M.T., Cecchini G., Manodori A., Ackrell B.A.C., Schröder I., Gunsalus R.P., Johnson M.K. Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster. Proc. Natl. Acad. Sci. 87:1990;8965-8969.