CO-dependent H2 evolution by Rhodospirillum rubrum: Role of CODH:CooF complex

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1757, Issue 12, 2006, Pages 1582-1591

  Singer, Steven W ^a   Hirst, Marissa B ^a   Ludden, Paul W ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Carbon monoxide dehydrogenase; EPR; Hydrogen; Hydrogenase

Indexed keywords

CARBON DIOXIDE; CARBON MONOXIDE DEHYDROGENASE; DEUTERIUM; IRON SULFUR PROTEIN; ALDEHYDE DEHYDROGENASE; BACTERIAL PROTEIN; CARBON MONOXIDE; HYDROGEN; MULTIENZYME COMPLEX; MULTIPROTEIN COMPLEX; PROTEIN SUBUNIT;

AMINO ACID SEQUENCE; ARTICLE; COMPARATIVE STUDY; COMPLEX FORMATION; CONTROLLED STUDY; CYTOLYSIS; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ANALYSIS; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; RHODOSPIRILLUM RUBRUM; SEQUENCE HOMOLOGY; BACTERIAL GENE; CHEMISTRY; GENETICS; METABOLISM; REGULON;

PHOTOBACTERIA; RHODOSPIRILLUM RUBRUM;

ALDEHYDE OXIDOREDUCTASES; BACTERIAL PROTEINS; CARBON MONOXIDE; ELECTRON SPIN RESONANCE SPECTROSCOPY; GENES, BACTERIAL; HYDROGEN; MULTIENZYME COMPLEXES; MULTIPROTEIN COMPLEXES; PROTEIN SUBUNITS; REGULON; RHODOSPIRILLUM RUBRUM;

EID: 33751531181     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.10.003     Document Type: Article

References (47)

1. Levin D.B., Pitt L., and Love M. Biohydrogen production: prospects and limitations to practical application. Int. J. Hydrogen Energy 29 (2004) 173-185
2. Das D., and Veziroglu T.N. Hydrogen production by biological processes: a survey of literature. Int. J. Hydrogen Energy 26 (2001) 13-28
3. Hallenbeck P.C., and Benemann J.R. Biological hydrogen production; fundamentals and limiting processes. Int. J. Hydrogen Energy 27 (2002) 1185-1193
4. Maness P.C., and Weaver P.F. Evidence for three distinct hydrogenase activities in Rhodospirillum rubrum. Appl. Microbiol. Biotechnol. 57 (2001) 751-756
5. Kerby R.L., Ludden P.W., and Roberts G.P. Carbon monoxide-dependent growth of Rhodospirillum rubrum. J. Bacteriol. 177 (1995) 2241-2244
6. Kerby R.L., Ludden P.W., and Roberts G.P. In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: molecular and physiological characterization of CooCTJ. J. Bacteriol. 179 (1997) 2259-2266
7. Shelver D., Kerby R.L., He Y.P., and Roberts G.P. Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of CooA, a member of the cyclic-AMP receptor protein family of transcriptional regulators. J. Bacteriol. 177 (1995) 2157-2163
8. Kerby R.L., Hong S.S., Ensign S.A., Coppoc L.J., Ludden P.W., and Roberts G.P. Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system. J. Bacteriol. 174 (1992) 5284-5294
9. Fox J.D., He Y.P., Shelver D., Roberts G.P., and Ludden P.W. Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum. J. Bacteriol. 178 (1996) 6200-6208
10. Bonam D., and Ludden P.W. Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum. J. Biol. Chem. 262 (1987) 2980-2987
11. Drennan C.L., Heo J.Y., Sintchak M.D., Schreiter E., and Ludden P.W. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc. Nat. Acad. Sci. U. S. A. 98 (2001) 11973-11978
12. 4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. Nat. Struct. Biol. 10 (2003) 271-279
13. Dobbek H., Svetlitchnyi V., Gremer L., Huber R., and Meyer O. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science 293 (2001) 1281-1285
14. Hedderich R. Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I. J. Bioenerg. Biomem. 36 (2004) 65-75
15. Fox J.D., Kerby R.L., Roberts G.P., and Ludden P.W. Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme. J. Bacteriol. 178 (1996) 1515-1524
16. Maness P.C., Huang J., Smolinski S., Tek V., and Vanzin G. Energy generation from the CO oxidation-hydrogen production pathway in Rubrivivax gelatinosus. App. Environ. Microbiol. 71 (2005) 2870-2874
17. Sapra R., Bagramyan K., and Adams M.W.W. A simple energy-conserving system: proton reduction coupled to proton translocation. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 7545-7550
18. 2 evolution system of Rhodospirillum rubrum-role of a 22-KDa iron-sulfur protein in mediating electron transfer between carbon monoxide dehydrogenase and hydrogenase. J. Biol. Chem. 266 (1991) 18395-18403
19. Klasson K.T., Lundback K.M.O., Clausen E.C., and Gaddy J.L. Kinetics of light limited growth and biological hydrogen production from carbon monoxide and water by Rhodospirillum rubrum. J. Biotechnol. 29 (1993) 177-188
20. 2-evolving enzyme complex from Carboxydothermus hydrogenoformans. Eur. J. Biochem. 269 (2002) 5712-5721
21. Bonam D., Murrell S.A., and Ludden P.W. Carbon monoxide dehydrogenase from Rhodospirillum rubrum. J. Bacteriol. 159 (1984) 693-699
22. Ensign S.A., Hyman M.R., and Ludden P.W. Nickel-specific, slow-binding inhibition of carbon monoxide dehydrogenase from Rhodospirillum rubrum by cyanide. Biochemistry 28 (1989) 4973-4979
23. Ensign S.A., Campbell M.J., and Ludden P.W. Activation of the nickel-deficient carbon monoxide dehydrogenase from Rhodospirillum rubrum-Kinetic characterization and reductant requirement. Biochemistry 29 (1990) 2162-2168
24. Ludden P.W., and Burris R.H. Activating factor for iron protein of nitrogenase from Rhodospirillum rubrum. Science 194 (1976) 424-426
25. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
26. Blake M.S., Johnston K.H., Russell-Jones G.J., and Gotschlich E.C. A rapid, sensitive method for detection of alkaline-phosphatase conjugated anti-antibody on western blots. Anal. Biochem. 136 (1984) 175-179
27. Smith P.K., Krohn R.I., Hermanson G.T., Mallia A.K., Gartner F.H., Provenzano M.D., Fujimoto E.K., Goeke N.M., Olson B.J., and Klenk D.C. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150 (1985) 76-85
28. Spangler N.J., Lindahl P.A., Bandarian V., and Ludden P.W. Spectroelectrochemical characterization of the metal centers in carbon monoxide dehydrogenase (CODH) and nickel-deficient CODH from Rhodospirillum rubrum. J. Biol. Chem. 271 (1996) 7973-7977
29. Heo J., Staples C.R., Telser J., and Ludden P.W. Rhodospirillum rubrum CO-dehydrogenase. Part 2. Spectroscopic investigation and assignment of spin-spin coupling signals. J. Am. Chem. Soc. 121 (1999) 11045-11057
30. Smith E.T., Ensign S.A., Ludden P.W., and Feinberg B.A. Direct electrochemical studies of hydrogenase and CO dehydrogenase. Biochem. J. 285 (1992) 181-185
31. Craft J.L., Ludden P.W., and Brunold T.C. Spectroscopic studies of nickel-deficient carbon monoxide dehydrogenase from Rhodospirillum rubrum: nature of the iron-sulfur clusters. Biochemistry 41 (2002) 1681-1688
32. Hu Z.G., Spangler N.J., Anderson M.E., Xia J.Q., Ludden P.W., Lindahl P.A., and Munch E. Nature of the C-cluster in Ni-containing carbon monoxide dehydrogenases. J. Am. Chem. Soc. 118 (1996) 830-845
33. Mathews R., Charlton S., Sands R.H., and Palmer G. Nature of spin coupling between iron-sulfur clusters in 8-Fe ferredoxins. J. Biol. Chem. 249 (1974) 4326-4328
34. Reyntjens B., Jollie D.R., Stephens P.J., GaoSheridan H.S., and Burgess B.K. Purification and characterization of a FixABCX-linked 2[4Fe-4S] ferredoxin from Azotobacter vinelandii. J. Biol. Inorg. Chem. 2 (1997) 595-602
35. Koch H.G., Kern M., and Klemme J.H. Reinvestigation of regulation of biosynthesis and subunit composition of nickel-dependent Hup-hydrogenase of Rhodospirillum rubrum. FEMS Microbiol. Lett. 91 (1992) 193-197
36. Heo J.Y., Staples C.R., Halbleib C.M., and Ludden P.W. Evidence for a ligand CO that is required for catalytic activity of CO dehydrogenase from Rhodospirillum rubrum. Biochemistry 39 (2000) 7956-7963
37. Carter K.R., Rawlings J., Orme-Johnson W.H., Becker R.R., and Evans H.J. Purification and characterization of a ferredoxin from Rhizobium japonicum bacteroids. J. Biol. Chem. 255 (1980) 4213-4223
38. Fraser D.M., and Lindahl P.A. Stoichiometric CO reductive titrations of acetyl-CoA synthase (carbon monoxide dehydrogenase) from Clostridium thermoaceticum. Biochemistry 38 (1999) 15697-15705
39. Lindahl P.A. The Ni-containing carbon monoxide dehydrogenase family: light at the end of the tunnel?. Biochemistry 41 (2002) 2097-2105
40. Svetlitchnyi V., Peschel C., Acker G., and Meyer O. Two membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans. J. Bacteriol. 183 (2001) 5134-5144
41. Feng J., and Lindahl P.A. Effect of sodium sulfide on Ni-containing carbon monoxide dehydrogenases. J. Am. Chem. Soc. 126 (2004) 9094-9100
42. Jormakka M., Tornroth S., Byrne B., and Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295 (2002) 1863-1868
43. Jormakka M., Richardson D., Byrne B., and Iwata S. Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes. Structure 12 (2004) 95-104
44. Weiner J.H., Rothery R.A., Sambasivarao D., and Trieber C.A. Molecular analysis of dimethylsulfoxide reductase-a complex iron-sulfur molybdoenzyme of Escherichia coli. Biochim. Biophys. Acta 1102 (1992) 1-18
45. Olmo-Mira M.F., Gavira M., Richardson D.J., Castillo F., Moreno-Vivian C., and Roldan M.D. NapF is a cytoplasmic iron-sulfur protein required for Fe-S cluster assembly in the periplasmic nitrate reductase. J. Biol. Chem. 279 (2004) 49727-49735
46. Yagi T., and Hatefi Y. Identification of the dicyclohexylcarbodiimide-binding subunit of NADH-Ubiquinone oxidoreductase (Complex I). J. Biol. Chem. 263 (1988) 16150-16155
47. Forzi L., Koch J., Guss A.M., Radosevich C.G., Metcalf W.W., and Hedderich R. Assignment of the [4Fe-4S] clusters of Ech hydrogenase from Methanosarcina barkeri to individual subunits via the characterization of site-directed mutants. FEBS J. 272 (2005) 4741-4753