The [Ni-Fe] hydrogenase from the thermophilic bacterium Acetomicrobium flavidum

References

1. Adams M.W.W. The structure and mechanism of iron-hydrogenases. Biochim Biophys Acta 1990; 1020:115–145
   [Google Scholar]
2. Armengaud J., Jouanneau Y. Overexpression in Escherichia coli of the fdxA gene encoding Khodobacter capsulatus ferredoxin II. Protein Expr Purif 1995; 6:176–184
   [Google Scholar]
3. Atherton E., Sheppard R.C. Solid Phase Peptide Synthesis: a Practical Approach 1989 Oxford: IRL Press;
   [Google Scholar]
4. Bbhm R., Sauter M., Bdck A. Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol Microbiol 1990; 4:231–243
   [Google Scholar]
5. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248–254
   [Google Scholar]
6. De Boer H., Comstock H.L., Vasser V. The tac promoter: a functional hybrid derived from the trp and lac promoter. Proc Natl Acad Set USA 1983; 80:21–25
   [Google Scholar]
7. Dower W.J., Miller J.F., Ragsdale C.W. High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Ri-r 1988; 16:6127–6145
   [Google Scholar]
8. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
   [Google Scholar]
9. Legendre N., Matsudaira P. Gel electrophoresis. In A Practical Guide to Protein and Peptide Purification for Microsequencing 1989 Edited by Matsudaira P. San Diego: Academic Press; pp 52–69
   [Google Scholar]
10. Pedroni P., Della Volpe A., Galli G., Mura G.M., Pratesi C., Grandi G. Characterization of the locus encoding the (Ni-Fe) sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases. Microbiology 1995; 141:449–458
    [Google Scholar]
11. Pilkington S.J., Skehel J.M., Gennis R.B., Walker J.E. Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase. Biochemistry 1991; 30:2166–2175
    [Google Scholar]
12. Przybyla A.E., Robbins J., Menon N., Peck H.D. Jr Structure-function relationship among the nickel-containing hydrogenases. FEMS Microbiol Rev 1992; 88:109–136
    [Google Scholar]
13. Rossmann R., Maier T., Lottspeich F., Bdck A. Characterisation of a protease from Escherichia coli involved in hydrogenase maturation. Eur J Biochem 1995; 227:545–550
    [Google Scholar]
14. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: a Laboratory Manual, 2nd edn 1989 Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
15. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 1977; 74:5463–5467
    [Google Scholar]
16. Schindler F., Winter J. Purification and properties of a soluble, thermophilic hydrogenase of Acetomicrobium flavidum. Biochim Biophys Acta 1987; 913:81–88
    [Google Scholar]
17. Schuler G.D., Altschul S.F., Lipman D.J. A workbench for multiple alignment construction and analysis. Proteins 1991; 9:180–190
    [Google Scholar]
18. Soutschek E., Winter J., Schindler F., Kandler O. Acetomicrobium flavidum, gen. nov., sp. nov., a thermophilic, anaerobic bacterium from sewage sludge, forming acetate, CO, 2 and H2 from glucose. Syst Appl Microbiol 1984; 5:377–390
    [Google Scholar]
19. Tran-Betcke A., Warnecke U., Bocker C., Zaborosch C., Friedrich B. Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus HI6. J Bacteriol 1990; 172:2920–2929
    [Google Scholar]
20. Veber D.F., Milkowsky J.D., Varga S.L., Denkewalter R.G., Hirschmann R. Acetamidomethyl. A novel thiol protecting group for cysteine. J Am Chem Soc 1972; 94:5456–5461
    [Google Scholar]
21. Vignais P.M., Toussaint B. Molecular biology of membrane-bound H2 uptake hydrogenases. Arch Microbiol 1994; 161:1–10
    [Google Scholar]
22. 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 1995; 373:580–587
    [Google Scholar]
23. Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H. The gene locus of the proton-translocating NADH-ubiquinone oxidoreductase in Escherichia coli. J Mol Biol 1993; 233:109–122
    [Google Scholar]
24. Wu L.-F., Mandrand M.A. Microbial hydrogenases: primary structure, classification signatures and phylogeny. FEMS Microbiol Rev 1993; 104:243–270
    [Google Scholar]
25. Xu X., Matsuno-Yagi A., Yagi T. Gene cluster of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans: characterization of four structural gene products. Biochemistry 1992; 31:6925–6932
    [Google Scholar]