A universal scaffold for synthesis of the Fe(CN)2(CO) moiety of [NiFe] hydrogenase

Journal of Biological Chemistry

Volumn 287, Issue 46, 2012, Pages 38845-38853

  Bürstel, Ingmar ^a   Sieberts, Elisabeth ^b   Winter, Gordon ^a,c   Hummels, Philipp ^b   Zebgers, Ingo ^b   Friedrich, Bärbel ^a   Lenz, Oliver ^a  

^a HUMBOLDT UNIVERSITY   (Germany)

^b TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

^c UNIVERSITY HOSPITAL ULM   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

[NIFE]-HYDROGENASE; ASSEMBLY PROCESS; CATALYTIC CENTER; CO LIGANDS; COFACTORS; CYSTEINE RESIDUES; DINUCLEAR; EXPERIMENTAL EVIDENCE; HYDROGENASES; IN-VIVO; INFRARED SPECTROSCOPIC ANALYSIS; IRON IONS; MUTANT ANALYSIS; RALSTONIA EUTROPHA;

AMINO ACIDS; BACTERIA; BIOSYNTHESIS; CARBON MONOXIDE; CYANIDES; ESCHERICHIA COLI; GENETIC ENGINEERING; HYDROGEN; METAL IONS; PROTEINS; SPECTROSCOPIC ANALYSIS;

LIGANDS;

CARBON MONOXIDE; CYANIDE; CYSTEINE; HYPC PROTEIN; HYPD PROTEIN; IRON; NICKEL IRON HYDROGENASE; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CUPRIAVIDUS NECATOR; ENZYME ACTIVE SITE; ESCHERICHIA COLI; GENETIC ENGINEERING; IN VIVO STUDY; INFRARED SPECTROSCOPY; LIGAND BINDING; MOLECULAR INTERACTION; MUTATIONAL ANALYSIS; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; UPREGULATION;

BACTERIAL PROTEINS; CARBON MONOXIDE; CATALYTIC DOMAIN; CUPRIAVIDUS NECATOR; CYANIDES; CYSTEINE; DNA MUTATIONAL ANALYSIS; ESCHERICHIA COLI; GENETIC ENGINEERING; HYDROGENASE; IONS; IRON; LIGANDS; METALS; PROTEINS;

CUPRIAVIDUS NECATOR; ESCHERICHIA COLI;

EID: 84869029258     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.376947     Document Type: Article

References (38)

1. Jones, A. K., Lenz, O., Strack, A., Buhrke, T., and Friedrich, B. (2004) NiFe hydrogenase active site biosynthesis. Identification of Hyp protein complexes in Ralstonia eutropha. Biochemistry 43, 13467-13477 (Pubitemid 39391148)
2. Forzi, L., and Sawers, R. G. (2007) Maturation of [NiFe] hydrogenases in Escherichia coli. Biometals 20, 565-578 (Pubitemid 46776563)
3. Böck, A., King, P. W., Blokesch, M., and Posewitz, M. C. (2006) Maturation of hydrogenases. Adv. Microb. Physiol. 51, 1-71
4. Blokesch, M., and Böck, A. (2006) Properties of the [NiFe] hydrogenase maturation protein HypD. FEBS Lett. 580, 4065-4068 (Pubitemid 44037570)
5. Watanabe, S., Matsumi, R., Arai, T., Atomi, H., Imanaka, T., and Miki, K. (2007) Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE. Insights into cyanation reaction by thiol redox signaling. Mol. Cell 27, 29-40 (Pubitemid 46991387)
6. Blokesch, M., Albracht, S. P., Matzanke, B. F., Drapal, N. M., Jacobi, A., and Böck, A. (2004) The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe] hydrogenases. J. Mol. Biol. 344, 155-167 (Pubitemid 39422380)
7. Reissmann, S., Hochleitner, E., Wang, H., Paschos, A., Lottspeich, F., Glass, R. S., and Böck, A. (2003) Taming of a poison. Biosynthesis of the [NiFe] hydrogenase cyanide ligands. Science 299, 1067-1070 (Pubitemid 36222933)
8. Petkun, S., Shi, R., Li, Y., Asinas, A., Munger, C., Zhang, L., Waclawek, M., Soboh, B., Sawers, R. G., and Cygler, M. (2011) Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sites. Structure 19, 1773-1783
9. Blokesch, M., Paschos, A., Bauer, A., Reissmann, S., Drapal, N., and Böck, A. (2004) Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE. Eur. J. Biochem. 271, 3428-3436 (Pubitemid 39120342)
10. 2 as performed by the membrane-bound [NiFe] hydrogenase of Ralstonia eutropha. Chemphyschem. 11, 1107-1119
11. Ludwig, M., Schubert, T., Zebger, I., Wisitruangsakul, N., Saggu, M., Strack, A., Lenz, O., Hildebrandt, P., and Friedrich, B. (2009) Concerted action of two novel auxiliary proteins in assembly of the active site in a membrane-bound [NiFe] hydrogenase. J. Biol. Chem. 284, 2159-2168
12. Kaluarachchi, H., Zhang, J. W., and Zamble, D. B. (2011) Escherichia coli SlyD, more than a Ni(II) reservoir. Biochemistry 50, 10761-10763
13. Chung, K. C., and Zamble, D. B. (2011) The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe] hydrogenase 3. FEBS Lett. 585, 291-294
14. Thiemermann, S., Dernedde, J., Bernhard, M., Schroeder, W., Massanz, C., and Friedrich, B. (1996) Carboxyl-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eutrophus requires the hoxW gene product. J. Bacteriol. 178, 2368-2374 (Pubitemid 26123502)
15. Magalon, A., Blokesch, M., Zehelein, E., and Böck, A. (2001) Fidelity of metal insertion into hydrogenases. FEBS Lett. 499, 73-76 (Pubitemid 32539324)
16. Bürstel, I., Hummel, P., Siebert, E., Wisitruangsakul, N., Zebger, I., Friedrich, B., and Lenz, O. (2011) Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase. J. Biol. Chem. 286, 44937-44944
17. -, but not of the intrinsic CO in the active site of the regulatory [NiFe] hydrogenase from Ralstonia eutropha. FEBS Lett. 581, 3322-3326
18. - ligands to the active site Fe in [NiFe] hydrogenase of Escherichia coli have different metabolic origins. FEBS Lett. 581, 3317-3321
19. Schwartz, E., and Friedrich, B. (2006) in The Prokaryotes (Dworkin, M., ed) Vol. 2, 3rd Ed., pp. 496-564, Springer-Verlag, New York
20. Srivastava, S., Urban, M., and Friedrich, B. (1982) Mutagenesis of Alcaligenes eutrophus by insertion of the drug-resistance transposon Tn5. Arch. Microbiol. 131, 203-207 (Pubitemid 12066922)
21. Schwartz, E., Gerischer, U., and Friedrich, B. (1998) Transcriptional regulation of Alcaligenes eutrophus hydrogenase genes. J. Bacteriol. 180, 3197-3204 (Pubitemid 28285035)
22. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
23. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354 (Pubitemid 9256559)
24. Schink, B., and Schlegel, H. G. (1979) The membrane-bound hydrogenase of Alcaligenes eutrophus. I. Solubilization, purification, and biochemical properties. Biochim. Biophys. Acta 567, 315-324
25. Friedrich, B., Heine, E., Finck, A., and Friedrich, C. G. (1981) Nickel requirement for active hydrogenase formation in Alcaligenes eutrophus. J. Bacteriol. 145, 1144-1149 (Pubitemid 11097330)
26. Schwarze, A., Kopczak, M. J., Rögner, M., and Lenz, O. (2010) Requirements for construction of a functional hybrid complex of photosystem I and [NiFe] hydrogenase. Appl. Environ. Microbiol. 76, 2641-2651
27. Priefert, H., Hein, S., Krüger, N., Zeh, K., Schmidt, B., and Steinbüchel, A. (1991) Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism. J. Bacteriol. 173, 4056-4071
28. Wolf, I., Buhrke, T., Dernedde, J., Pohlmann, A., and Friedrich, B. (1998) Duplication of hyp genes involved in maturation of [NiFe] hydrogenases in Alcaligenes eutrophus H16. Arch. Microbiol. 170, 451-459 (Pubitemid 28523650)
29. Dernedde, J., Eitinger, T., Patenge, N., and Friedrich, B. (1996) hyp gene products in Alcaligenes eutrophus are part of a hydrogenase-maturation system. Eur. J. Biochem. 235, 351-358
30. Dernedde, J., Eitinger, M., and Friedrich, B. (1993) Analysis of a pleiotropic gene region involved in formation of catalytically active hydrogenases in Alcaligenes eutrophus H16. Arch. Microbiol. 159, 545-553 (Pubitemid 23169542)
31. Pandelia, M. E., Ogata, H., and Lubitz, W. (2010) Intermediates in the catalytic cycle of [NiFe] hydrogenase. Functional spectroscopy of the active site. Chemphyschem. 11, 1127-1140
32. De Lacey, A. L., Fernandez, V. M., Rousset, M., and Cammack, R. (2007) Activation and inactivation of hydrogenase function and the catalytic cycle. Spectroelectrochemical studies. Chem. Rev. 107, 4304-4330 (Pubitemid 350041746)
33. Tard, C., and Pickett, C. J. (2009) Structural and functional analogues of the active sites of the [Fe], [NiFe], and [FeFe] hydrogenases. Chem. Rev. 109, 2245-2274
34. Roseboom, W., Blokesch, M., Böck, A., and Albracht, S. P. (2005) The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different. FEBS Lett. 579, 469-472 (Pubitemid 40092428)
35. Rauchfuss, T. B., Contakes, S. M., Hsu, S. C., Reynolds, M. A., and Wilson, S. R. (2001) The influence of cyanide on the carbonylation of iron(II). Synthesis of Fe-Sr-Cn-Co centers related to the hydrogenase active sites. J. Am. Chem. Soc. 123, 6933-6934 (Pubitemid 32884557)
36. Nakamoto, K. (2008) Infrared and Raman Spectra of Inorganic and Coordination Compounds, pp. 403-408, John Wiley & Sons, Inc., New York
37. Moreland, A. C., and Rauchfuss, T. B. (2000) Binding of π-acceptor ligands to (triamine)iron(II) complexes. Inorg. Chem. 39, 3029-3036
38. Gordon, J. C., and Kubas, G. J. (2010) Perspectives on how nature employs the principles of organometallic chemistry in dihydrogen activation in hydrogenases. Organometallics 29, 4682-4701