Cryogenic and laser photoexcitation studies identify multiple roles for active site residues in the light-driven enzyme protochlorophyllide oxidoreductase

Journal of Biological Chemistry

Volumn 284, Issue 27, 2009, Pages 18160-18166

  Menon, Binuraj R K ^a   Waltho, Jonathan P ^a   Scrutton, Nigel S ^a   Heyes, Derren J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED ENZYMES; ACTIVE SITE RESIDUES; CATALYTIC ACTIVITY; CHLOROPHYLL BIOSYNTHESIS; CONSERVED RESIDUES; DOUBLE BONDS; ENZYME ACTIVE SITES; HYDRIDE TRANSFERS; LOW TEMPERATURE FLUORESCENCE; OVERALL REACTIONS; PROTOCHLOROPHYLLIDE; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; PROTON DONORS; REACTION MECHANISM; SHORT CHAIN ALCOHOLS; SUBSTRATE BINDING; TERNARY ENZYMES;

BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CATALYSTS; CHLOROPHYLL; ENZYMES; EXCITED STATES; FLUORESCENCE SPECTROSCOPY; HYDROGEN; PHOTOEXCITATION; PORPHYRINS;

PROTON TRANSFER;

HYDROGEN; LYSINE; OXIDOREDUCTASE; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CYANOBACTERIUM; ENZYME SUBSTRATE; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HYDROGEN BOND; LASER; LOW TEMPERATURE; MUTAGENESIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; STEADY STATE;

CATALYTIC DOMAIN; COLD TEMPERATURE; FLUORESCENCE; KINETICS; LASERS; LIGHT; LYSINE; MUTAGENESIS; NADP; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PHOTOCHEMICAL PROCESSES; PROTEIN STRUCTURE, TERTIARY; PROTONS; SYNECHOCOCCUS; TYROSINE;

EID: 67650538081     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.020719     Document Type: Article

References (39)

1. Heyes, D. J., and Hunter, C. N. (2005) Trends Biochem. Sci. 30, 642-649
2. Lebedev, N., and Timko, M. P. (1998) Photosynth. Res. 58, 5-23
3. Masuda, T., and Takamiya, K. (2004) Photosynth. Res. 81, 1-29
4. Bröcker, M. J., Virus, S., Ganskow, S., Heathcote, P., Heinz, D. W., Schubert, W. D., Jahn, D., and Moser, J. (2008) J. Biol. Chem. 283, 10559-10567
5. Mees, A., Klar, T., Gnau, P., Hennecke, U., Eker, A. P., Carell, T., and Essen, L. O. (2004) Science 306, 1789-1793
6. Valera, V., Fung, M., Wessler, A. N., and Richards, W. R. (1987) Biochem. Biophys. Res. Commun. 148, 515-520
7. Begley, T. P., and Young, H. (1989) J. Am. Chem. Soc. 111, 3095-3096
8. Wilks, H. M., and Timko, M. P. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 724-728
9. Heyes, D. J., Ruban, A. V., Wilks, H. M., and Hunter, C. N. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 11145-11150
10. Heyes, D. J., Ruban, A. V., and Hunter, C. N. (2003) Biochemistry 42, 523-528
11. Heyes, D. J., and Hunter, C. N. (2004) Biochemistry 43, 8265-8271
12. Heyes, D. J., Heathcote, P., Rigby, S. E., Palacios, M. A., van Grondelle, R., and Hunter, C. N. (2006) J. Biol. Chem. 281, 26847-26853
13. Heyes, D. J., Sakuma, M., de Visser, S. P., and Scrutton, N. S. (2009) J. Biol. Chem. 284, 3762-3767
14. Heyes, D. J., Sakuma, M., and Scrutton, N. S. (2007) J. Biol. Chem. 282, 32015-32020
15. Heyes, D. J., Hunter, C. N., van Stokkum, I. H., van Grondelle, R., and Groot, M. L. (2003) Nat. Struct. Biol. 10, 491-492
16. Dietzek, B., Kiefer, W., Hermann, G., Popp, J., and Schmitt, M. (2006) J. Phys. Chem. B 110, 4399-4406
17. Zhao, G. J., and Han, K. L. (2008) Biophys. J. 94, 38-46
18. Sytina, O. A., Heyes, D. J., Hunter, C. N., Alexandre, M. T., van, Stokkum, I. H., van, Grondelle, R., and Groot, M. L. (2008) Nature 456, 1001-1004
19. Dietzek, B., Tschierlei, S., Hermann, G., Yartsev, A., Pascher, T., Sundström, V., Schmitt, M., and Popp, J. (2009) Chemphyschem. 10, 144-150
20. Oppermann, U., Filling, C., Hult, M., Shafqat, N., Wu, X., Lindh, M., Shafqat, J., Nordling, E., Kallberg, Y., Persson, B., and Jörnvall, H. (2003) Chem. Biol. Interact. 143-144, 247-253
21. Hammes-Schiffer, S. (2002) Biochemistry 41, 13335-13343
22. Benkovic, S. J., and Hammes-Schiffer, S. (2003) Science 301, 1196-1202
23. Boehr, D. D., McElheny, D., Dyson, H. J., and Wright, P. E. (2006) Science 313, 1638-1642
24. Kohen, A., Cannio, R., Bartolucci, S., and Klinman, J. P. (1999) Nature 399, 496-499
25. Kohen, A., and Klinman, J. P. (2000) J. Am. Chem. Soc. 122, 10738-10739
26. Sutcliffe, M. J., and Scrutton, N. S. (2000) Trends Biochem. Sci. 25, 405-408
27. Townley, H. E., Sessions, R. B., Clarke, A. R., Dafforn, T. R., and Griffiths, W. T. (2001) Proteins 44, 329-335
28. Ensor, C. M., and Tai, H. H. (1991) Biochem. Biophys. Res. Commun. 176, 840-845
29. Obeid, J., and White, P. C. (1992) Biochem. Biophys. Res. Commun. 188, 222-227
30. Chen, Z., Jiang, J. C., Lin, Z. G., Lee, W. R., Baker, M. E., and Chang, S. H. (1993) Biochemistry 32, 3342-3346
31. Varughese, K. I., Xuong, N. H., Kiefer, P. M., Matthews, D. A., and Whiteley, J. M. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 5582-5586
32. Lebedev, N., Karginova, O., McIvor, W., and Timko, M. P. (2001) Biochemistry 40, 12562-12574
33. Heyes, D. J., and Hunter, C. N. (2002) Biochem. Soc. Trans. 30, 601-604
34. Heyes, D. J., Menon, B. R., Sakuma, M., and Scrutton, N. S. (2008) Biochemistry 47, 10991-10998
35. McFarlane, M. J., Hunter, C. N., and Heyes, D. J. (2005) Photochem. Photobiol. Sci. 4, 1055-1059
36. Henneke, C. M., and Wedding, R. T. (1975) Arch. Biochem. Biophys. 168, 436-442
37. Jiménez, M. C., Miranda, M. A., and Tormos, R. (2005) Chem. Soc. Rev. 34, 783-796
38. Deonarain, M. P., Berry, A., Scrutton, N. S., and Perham, R. N. (1989) Biochemistry 28, 9602-9607
39. Zheng, Y. J., and Ornstein, R. L. (1997) J. Am. Chem. Soc. 119, 1523-1528