Enzymatic properties and effect of ionic strength on periplasmic nitrate reductase (NAP) from Desulfovibrio desulfuricans ATCC 27774

Biochemical and Biophysical Research Communications

Volumn 239, Issue 3, 1997, Pages 816-822

  Bursakov, S A ^a,b   Carneiro, C ^a   Almendra, M J ^a   Duarte, R O ^a   Caldeira, J ^a   Moura, I ^a   Moura, J J G ^a  

^a UNIVERSIDADE NOVA DE LISBOA   (Portugal)

^b BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

Author keywords

Desulfovibrio desulfuricans ATCC 27774; Iron sulfur cluster; Molybdenum; Molybdenum enzymes; Molybdopterin guanine dinucleotide; Nitrate reductase

Indexed keywords

CALCIUM ION; CYANIDE; FERRICYANIDE; GUANINE DERIVATIVE; MAGNESIUM ION; METALLOPROTEIN; MOLYBDENUM; NITRATE REDUCTASE; NITRITE REDUCTASE; PHOSPHATE; POTASSIUM ION; PTERIN DERIVATIVE; SODIUM ION; SULFATE;

AMINO TERMINAL SEQUENCE; ARTICLE; COENZYME; DESULFOVIBRIO; ELECTRON SPIN RESONANCE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME INHIBITION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IONIC STRENGTH; MOLECULAR WEIGHT; NONHUMAN; OXIDATION; PRIORITY JOURNAL;

DESULFOVIBRIO; DESULFOVIBRIO DESULFURICANS; NEUROSPORA CRASSA;

EID: 0031590434     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1997.7560     Document Type: Article

References (53)

1. Postgate J. R. The Sulfate-Reducing Bacteria. 1984;Cambridge University Press. p. 42-43.
2. Fauque G. D. Sulfate Reducing Bacteria. 1995;Plenum Press, New York. p. 217-241.
3. Senez J. C., Pichinoty F. Bull. Soc. Chim. Biol. Paris. 40:1958;2099-2117.
4. Liu M. C., Peck H. D. Jr. J. Biol. Chem. 256:1981;13159-13164.
5. McCready R. G. L., Gould W. D., Cook F. D. Arch. Microbiol. 135:1983;182-185.
6. Widdel F., Pfenning N. Arch. Microbiol. 131:1982;360-365.
7. Widdel F., Pfenning N. Krieg N. R., Holt J. G. Bergey's Manual of Systematic Bacteriology. 1984;663-679 Williams and Wilkins Co. Baltimore.
8. Bursakov S. A., Liu M-Y., Payne W. J., LeGall J., Moura I., Moura J. J. G. Anaerobe. 1:1995;55-60.
9. Coughlan M. P., Johnson J. L., Rajagopalan K. V. J. Biol. Chem. 255:1980;2694-2699.
10. Solomonson L. P. Biochem. Biophys. Acta. 334:1974;297-308.
11. Liu M. C., Peck H. D. Jr. J. Biol. Chem. 256:1981;13159-13164.
12. Lowe R. H., Evans H. J. Biochim. Biophys. Acta. 85:1964;377-389.
13. Garrett R. H., Nason A. J. Biol. Chem. 244:1969;2870-2882.
14. Bradford M. M. Anal. Biochem. 72:1976;248-254.
15. Lowry O. H., Rosenbrough N. J., Farr A. L., Randall R. J. J. Biol. Chem. 193:1951;265-275.
16. Hawkes T. R., Bray R. C. Biochem. J. 219:1984;481-493.
17. Mendel R. R. Phytochem. 22:1983;817-819.
18. Frunzke K., Meyer O. Bioforum. 14:1991;83.
19. Reichenbecher W., Rudiger A., Kroneck P. M. H., Shink B. Eur. J. Biochem. 237:1996;406-413.
20. von Hippel P. H., Schleich T. Timasheff S. N., Fasman G. D. Structure and Stability of Biological Macromolecules. 1969;417-574 Marcel Dekker, New York.
21. Terreblanca M., Meseguer I., Rodriguez-Valera F. J. Gen. Microbiol. 135:1989;2655-2661.
22. van Spanning R. J. M., Wansell-Bettenhaussen C. W., Oltmann L. F., Stouthamer A. H. Eur. J. Biochem. 169:1987;349-352.
23. Berks B. C., Stuart J. F., Moir J. W. B., Richardson D. J. Biochim. Biophys. Acta. 1232:1995;97-173.
24. P. Richterich, N. Lakey, G. Gryan, L. Jaehn, L. Mintz, K. Robinson, G. M. Church, 1993.
25. Siddiqui R. A., Warnecke-Eberz U., Hengsberger A., Schneider B., Kostka S., Friedrich B. J. Bacteriol. 175:1993;5867-5876.
26. Shuber A. P., Orr E. C., Recny M. A., Shendel P. F., May H. D., Schauer N. L., Ferry J. G. J.Biol.Chem. 261:1986;12942-12947.
27. Lin J. T., Goldman, Goldman, Stewart V. J. Bacteriol. 175:1993;2370-2378.
28. Krafft T., Bokranz M., Klimmek O., Schroder I., Fahrenholz F., Kojro E., Kroger A. Eur. J. Biochem. 206:1992;503-510.
29. Berg B. L., Li J., Heider J., Stewart V. J. Biol. Chem. 1266:1991;22380-22385.
30. Stan-Lotter H., Lang F. J. Jr., Hochstein L. I. Appl. Theor. Electrophor. 1:1989;147-153.
31. Lanyi J. K. Bacteriol. Rev. 38:1974;272-290.
32. Danson M. J., McQuattie A., Stevenson K. J. Biochemistry. 25:1986;3880-3884.
33. May B. P., Dennis P. P. J. Bacteriol. 169:1987;1417-1422.
34. Hochstein L. I., Lang F. Arch. Bioch. Biophys. 288:1991;380-385.
35. Marquez E. D., Brodie A. F. Biochim. Biophys. Acta. 321:1973;84-89.
36. Hipkin C. R., Kau D. A., Cannons A. C. J. Gen. Microbiol. 139:1993;473-478.
37. Tanford C. Physical Chemistry of Macromolecules. 1961;Wiley, New York.
38. Arakawa T., Timasheff S. N. Biochemistry. 23:1984;5912-5923.
39. Mikami B., Ida S. Biochim. Biophys. Acta. 791:1984;294-304.
40. Adams M. W. W., Mortenson L. E. J. Biol. Chem. 257:1982;1791-1799.
41. Tran-Betcke A., Warnecke C., Bocker C., Zaborosch C., Friedrich B. J. Bacteriol. 172:1990;2920-2929.
42. Bruschi M., Guerlesquin F. FEMS Microbiol. Rev. 54:1988;155-176.
43. M. J. Almeida, R. O. Duarte, M. J. Romão, I. Moura, J. J. G. Moura, 1996, 3rd Eur. Conf. Bioinorg. Chem. Noorwijkerhout, Netherlands.
44. Costa C., Teixeira M., LeGall J., Moura J. J. G., Moura I. J. Biol. Inorg. Chem. 2:1997;198-208.
45. Hille R. Chem. Rev. 96:1996;2757-2816.
46. Romão M. J., Archer M., Moura I., Moura J. J. G., LeGall J., Engh R., Schneider M., Hof P., Huber R. Science. 167:1995;1170-1176.
47. Massey V., Edmondson D. J. Biol. Chem. 245:1970;6595-6598.
48. Boyington J. C., Gladyshev V. N., Khangulov S. V., Stadtman T. C., Sun P. D. Science. 275:1997;1305-1308.
49. Knäblein J., Mann K., Ehlert S., Fonstein M., Huber R., Schneider F. J. Mol. Biol. 263:1996;40-52.
50. Schindelin H., Kisker C., Hilton J., Rajagopalan K. V., Rees D. C. Science. 272:1996;1615-1621.
51. C. Kisker, H. Schindelin, D. C. Rees, April 1997, Molybdenum Enzymes Meeting, Univ. Sussex.
52. Huber R., Hof P., Duarte R. O., Moura J. J. G., Moura I., Liu M-Y., LeGall J., Hille R., Archer M., Romão M. J. PNAS. 93:1996;8846-8861.
53. Schneider F., Löwe J., Huber R., Schindelin H., Kisker C., Knäblein J. J. Mol. Biol. 263:1996;53-69.