參考文獻 |
H. F. Sturt, R. E. Summons, K. Smith, M. Elvert, K. U. Hinrichs, Intact polar membrane lipids in prokaryotes and sediments deciphered by high-performance liquid chromatography/electrospray ionization multistage mass spectrometry--new biomarkers for biogeochemistry and microbial ecology. Rapid Commun Mass Spectrom 18, 617-628 (2004).
2. L. Chen et al., The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota. J Bacteriol 187, 4992-4999 (2005).
3. S. Berkner, D. Grogan, S. V. Albers, G. Lipps, Small multicopy, non-integrative shuttle vectors based on the plasmid pRN1 for Sulfolobus acidocaldarius and Sulfolobus solfataricus, model organisms of the (cren-)archaea. Nucleic Acids Res 35, e88 (2007).
4. S. K. Chunduru, G. T. Mrachko, K. C. Calvo, Mechanism of ketol acid reductoisomerase--steady-state analysis and metal ion requirement. Biochemistry 28, 486-493 (1989).
5. K. Thomazeau et al., Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose. Acta Crystallogr D Biol Crystallogr 56, 389-397 (2000).
6. S. Brinkmann-Chen, J. K. Cahn, F. H. Arnold, Uncovering rare NADH-preferring ketol-acid reductoisomerases. Metab Eng 26, 17-22 (2014).
7. R. Dumas, V. Biou, F. Halgand, R. Douce, R. G. Duggleby, Enzymology, structure, and dynamics of acetohydroxy acid isomeroreductase. Acc Chem Res 34, 399-408 (2001).
8. R. Dumas, M. C. Butikofer, D. Job, R. Douce, Evidence for two catalytically different magnesium-binding sites in acetohydroxy acid isomeroreductase by site-directed mutagenesis. Biochemistry 34, 6026-6036 (1995).
9. S. Atsumi, T. Hanai, J. C. Liao, Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels. Nature 451, 86-89 (2008).
10. F. Halgand et al., Characterization of the conformational changes of acetohydroxy acid isomeroreductase induced by the binding of Mg2+ ions, NADPH, and a competitive inhibitor. Biochemistry 38, 6025-6034 (1999).
11. H. J. Ahn et al., Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa. J Mol Biol 328, 505-515 (2003).
12. W. R. Taylor, A deeply knotted protein structure and how it might fold. Nature 406, 916-919 (2000).
13. S. Bastian et al., Engineered ketol-acid reductoisomerase and alcohol dehydrogenase enable anaerobic 2-methylpropan-1-ol production at theoretical yield in Escherichia coli. Metab Eng 13, 345-352 (2011).
14. S. Brinkmann-Chen et al., General approach to reversing ketol-acid reductoisomerase cofactor dependence from NADPH to NADH. Proc Natl Acad Sci U S A 110, 10946-10951 (2013).
15. R. Dumas et al., Isolation and kinetic properties of acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) chloroplasts overexpressed in Escherichia coli. Biochem J 288 ( Pt 3), 865-874 (1992).
16. R. Dumas et al., Interactions of plant acetohydroxy acid isomeroreductase with reaction intermediate analogues: correlation of the slow, competitive, inhibition kinetics of enzyme activity and herbicidal effects. Biochem J 301 ( Pt 3), 813-820 (1994).
17. S. Epelbaum, D. M. Chipman, Z. Barak, Metabolic effects of inhibitors of two enzymes of the branched-chain amino acid pathway in Salmonella typhimurium. J Bacteriol 178, 1187-1196 (1996).
18. X. H. Liu et al., Synthesis, bioactivity, theoretical and molecular docking study of 1-cyano-N-substituted-cyclopropanecarboxamide as ketol-acid reductoisomerase inhibitor. Bioorg Med Chem Lett 17, 3784-3788 (2007).
19. W. H. Bragg, The Analysis of Crystal Structure by X-Rays. Science 60, 139-149 (1924).
20. S. E. Ealick, Advances in multiple wavelength anomalous diffraction crystallography. Curr Opin Chem Biol 4, 495-499 (2000).
21. A. Vagin, A. Teplyakov, Molecular replacement with MOLREP. Acta Crystallogr D Biol Crystallogr 66, 22-25 (2010).
22. J. M. Guss et al., Phase determination by multiple-wavelength x-ray diffraction: crystal structure of a basic "blue" copper protein from cucumbers. Science 241, 806-811 (1988).
23. M. Benfatto et al., Multiple-scattering regime and higher-order correlations in x-ray-absorption spectra of liquid solutions. Phys Rev B Condens Matter 34, 5774-5781 (1986).
24. H. Walden, Selenium incorporation using recombinant techniques. Acta Crystallogr D 66, 352-357 (2010).
25. W. A. Hendrickson, C. M. Ogata, Phase determination from multiwavelength anomalous diffraction measurements. Method Enzymol 276, 494-523 (1997).
26. G. D. Fasman, Circular dichroism and the conformational analysis of biomolecules. The language of science (Plenum Press, New York, 1996), pp. ix, 738 p.
27. U. J. Meierhenrich et al., Circular dichroism of amino acids in the vacuum-ultraviolet region. Angew Chem Int Ed Engl 49, 7799-7802 (2010).
28. L. Whitmore, B. A. Wallace, Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases. Biopolymers 89, 392-400 (2008).
29. N. J. Greenfield, Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1, 2876-2890 (2006).
30. J. M. Bartlett, D. Stirling, A short history of the polymerase chain reaction. Methods Mol Biol 226, 3-6 (2003).
31. M. Uhlen, Affinity as a tool in life science. Biotechniques 44, 649-654 (2008).
32. S. Paul-Dauphin et al., Probing size exclusion mechanisms of complex hydrocarbon mixtures: The effect of altering eluent compositions. Energ Fuel 21, 3484-3489 (2007).
33. R. Tyagi, R. Lai, R. G. Duggleby, A new approach to ′megaprimer′ polymerase chain reaction mutagenesis without an intermediate gel purification step. Bmc Biotechnol 4, (2004).
34. L. H. Hansen, S. Knudsen, S. J. Sorensen, The effect of the lacY gene on the induction of IPTG inducible promoters, studied in Escherichia coli and Pseudomonas fluorescens. Curr Microbiol 36, 341-347 (1998).
35. A. Marbach, K. Bettenbrock, lac operon induction in Escherichia coli: Systematic comparison of IPTG and TMG induction and influence of the transacetylase LacA. J Biotechnol 157, 82-88 (2012).
36. A. A. Watson, C. A. O′Callaghan, Crystallization and X-ray diffraction analysis of human CLEC-2. Acta Crystallogr Sect F Struct Biol Cryst Commun 61, 1094-1096 (2005).
37. M. D. Winn et al., Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67, 235-242 (2011). |