Kinetics and mechanism of the acid transition of the active site in plastocyanin

Biochemistry

Volumn 46, Issue 50, 2007, Pages 14619-14628

  Hass, Mathias A S ^a   Christensen, Hans E M ^b   Zhang, Jingdong ^b   Led, Jens J ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; CHEMICAL RELAXATION; CRYSTALLOGRAPHY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; REACTION RATES;

ACTIVE SITE; BUFFER CONCENTRATION; PLASTOCYANIN;

BACTERIA;

ASPARAGINE; COPPER; CUPROUS ION; HISTIDINE; IMIDAZOLE; PHOSPHATE BUFFERED SALINE; PLASTOCYANIN;

ACIDITY; ARTICLE; BINDING SITE; CHEMICAL REACTION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CRYSTALLOGRAPHY; KINETICS; MEASUREMENT; MUTATION; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT;

ANABAENA; BACTERIAL PROTEINS; BINDING SITES; COPPER; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PLASTOCYANIN; PROTONS;

ANABAENA VARIABILIS; CYANOBACTERIA;

EID: 37249081125     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701446u     Document Type: Article

References (39)

1. Hope, A. B. (2000) Electron transfer amongst cytochrome f, plastocyanin and photosystem I: Kinetics and mechanisms, Biochim. Biophys. Acta 1456, 5-26.
2. Sigfridsson, K. (1998) Plastocyanin, an electron-transfer protein, Photosynth. Res. 57, 1-28.
3. Markley, J. L., Ulrich, E. L., Berg, S. P., and Krogmann, D. W. (1975) Nuclear Magnetic Resonance Studies of Copper Binding Sites of Blue Copper Proteins: Oxidized, Reduced, and Apoplastocyanin, Biochemistry 14, 4428-4433.
4. Battistuzzi, G., Borsari, M., Canters, G. W., de Waal, E., Leonardi, A., Ranieri, A., and Sola, M. (2002) Thermodynamics of the Acid Transition in Blue Copper Proteins, Biochemistry 41, 14293-14298.
5. Dennison, C., Lawler, A. T., and Kohzuma, T. (2002) Unusual Properties of Plastocyanin from the Fern Dryopteris crassirhizoma, Biochemistry 41, 552-560.
6. Hunter, D. M., McFarlane, W., Sykes, A. G., and Dennison, C. (2001) Effect of pH on the Self-Exchange Reactivity of the Plant Plastocyanin from Parsley, Inorg. Chem. 40, 354-360.
7. Hulsker, R., Mery, A., Thomassen, E. A., Ranieri, A., Sola, M., Verbeet, M. P., Kohzuma, T., and Ubbink, M. (2007) Protonation of a histidine copper ligand in fern plastocyanin, J. Am. Chem. Soc. 129, 4423-4429.
8. I) poplar plastocyanin at six pH values, J. Mol. Biol. 192, 361-387.
9. Canters, G. W., Kolczak, U., Armstrong, F., Jeuken, L. J. C., Camba, R., and Sola, M. (2000) The effect of pH and ligand exchange on the redox properties of blue copper proteins, Faraday Discuss. 116, 205-220.
10. Kramer, D. M., Sacksteder, C. A., and Cruz, J. A. (1999) How acidic is the lumen? Photosynth. Res. 60, 151-163.
11. 1H-NMR Study on the Blue Copper Protein Amicyanin from Thiobacillus versutus. Resonance Identifications, Structural Rearrangements and Determination of the Electron Self-Exchange Rate Constant, Eur. J. Biochem. 176, 213-223.
12. 1H NMR, J. Biol. Chem. 265, 2768-2774.
13. Battistuzzi, G., Borsari, M., Loschi, L., Ranieri, A., Sola, M., and B. Mondovì, A. M. (2001) Redox properties and acid-base equilibria of zucchini mavicyanin, J. Inorg. Biochem. 83, 223-227.
14. Dennison, C., Kohzuma, T., McFarlane, W., Suzuki, S., and Sykes, A. G. (1994) Reactivity of Pseudoazurin from Achromobacter cycloclastes with Inorganic Redox Partners and Related NMR and Electrochemical Studies, Inorg. Chem. 33, 3299-3305.
15. Jeuken, L. J. C., van Vliet, P., Verbeet, M. P., Camba, R., McEvoy, J. P., Armstrong, F. A., and Canters, G. W. (2000) Role of the Surface-Exposed and Copper-Coordinating Histidine in Blue Copper Proteins: The Electron-Transfer and Redox-Coupled Ligand Binding Properties of His117Gly Azurin, J. Am. Chem. Soc. 122, 12186-12194.
16. Butuyan, M. V., Toy-Palmer, A., Chung, J., Blake, R. C., II, Beroza, P., Case, D. A., and Dyson, H. J. (1996) NMR Solution Sturucture of Cu(I) Rusticyanin from Thiobacillus ferrooxidans: Structural Basis for the Extreme Acid Stability and Redox Potential, J. Mol. Biol. 263, 752-767.
17. Kojiro, C. L., and Markley, J. L. (1983) Connectivity of proton and carbon spectra of the blue copper protein, plastocyanin, established by two-dimensional nuclear magnetic resonance, FEBS Lett. 162, 52-56.
18. Armstrong, F. A., Hill, H. A. O., Oliver, B. N., and Whitford, D. (1985) Direct Electrochemistry of the Photosynthetic Blue Copper Protein Plastocyanin. Electrostatic promotion of Rapid Charge Transfer at the Edge-Oriented Pyrolytic Graphite Electrode, J. Am. Chem. Soc. 107, 1473-1476.
19. 15N NMR Relaxation and Chemical Shift: Conformational Exchange in Plastocyanin Induced by Histidine Protonations, J. Am. Chem. Soc. 126, 753-765.
20. Schmidt, L., Christensen, H. E. M., and Harris, P. (2006) 1.6 Å structure of plastocyanin from Anabaena variabilis, Acta Crystallogr. D62, 1022-1029.
21. Eigen, M. (1963) Protonenübertragung, Säure-Base-Katalyse und enzymatische Hydrolyse. Teil I: Elementarvorgänge, Angew. Chem. 75, 489-508.
22. Khalifah, R. G. (1973) Carbon Dioxide Hydration Activity of Carbonic Anhydrase: Paradoxical Consequences of the Unusully Rapid Catalysis, Proc. Natl. Acad. Sci. U.S.A. 70, 1986-1989.
23. Sudmeier, J. L., Evelhoch, J. L., and Jonsson, N. B.-H. (1980) Dependence of NMR Lineshape Analysis upon Chemical Rates and Mechanisms: Implications for Enzyme Histidine Titrations, J. Magn. Reson. 40, 377-390.
24. Kalverda, A. P., Ubbink, M., Gilardi, G., Wijmenga, S. S., Crawford, A., Jeuken, L. J. C., and Canters, G. W. (1999) Backbone Dynamics of Azurin in Solution: Slow Conformational Change Associated with Deprotonation of Histidine 35, Biochemistry 38, 12690-12697.
25. Dennison, C., and Lawler, A. T. (2001) Investigation of the Alkaline and Acid Transition of Umecyanin, a Stellacyanin from Horseradish Roots, Biochemistry 40, 3158-3166.
26. Sato, K., and Dennison, C. (2002) Effect of Histidine 6 Protonation on the Active Site Structure And Electron-Transfer Capabilities of Pseudoazurin from Achromobacter cycloclastes, Biochemistry 41, 120-130.
27. 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques, J. Biomol. NMR 4, 845-858.
28. 15N NMR Relaxation, Biochemistry 33, 5984-6003.
29. Hass, M. A. S., Jensen, M. R., and Led, J. J. (2007) Probing Electric Fields in Proteins in Solution by NMR (submitted for publication).
30. Hass, M. A. S., and Led, J. J. (2006) Evaluation of two simplified N-15-NMR methods for determining μs-ms dynamicsm of proteins, Magn. Reson. Chem. 44, 761-769.
31. Zhang, J., Chi, Q., Nielsen, J. U., Friis, E. P., Andersen, J. E. T., and Ulstrup, J. (2000) Two-dimensional cysteine and cystine cluster networks on Au(111) disclosed by voltametry and in situ scanning tunneling microscopy, Langmuir 16, 7229-7237.
32. Lindskog, S. (1997) Structure and Mechanism of Carbonic Anhydrase, Pharmacol. Ther. 74, 1-20.
33. Lindskog, S., and Coleman, J. E. (1973) The Catalytic Mechanism of Carbonic Anhydrase, Proc. Natl. Acad. Sci. U.S.A. 70, 2505-2508.
34. Fisher, Z., Prada, J. A. H., Tu, C., Duda, D., Yoshioka, C., An, H., Govindamy, L., Silverman, D. N., and McKenna, R. (2005) Structural and Kinetic Characterization of Active-Site Histidine as a Proton Shuttle in Catalysis by Human Carbonic Anhydrase II, Biochemistry 44, 1097-1105.
35. Iversen, G., Kharkats, I. Y., and Ulstrup, J. (1998) Simple Dielectric Image Charge Models for Electrostatic Interactions in Metalloproteins, Mol. Phys. 94, 297-306.
36. Bashford, D., Karplus, M., and Canters, G. W. (1988) Electrostatic Effects of Charge Perturbations Introduced by Metal Oxidation in Proteins, J. Mol. Biol. 203, 507-510.
37. deSilva, D. G. A. H., Beokubetts, D., Kyritsis, P., Govindaraju, K., Powls, R., Tomkinson, N. P., and Sykes, A. G. (1992) Protein Protein Cross-Reactions Involving Plastocyanin, Cytochrome-f and Azurin: Self-Exchange Rate Constant and Related Studies with Inorganic Complexes, J. Chem. Soc., Dalton Trans. 14, 2145-2151.
38. McLeod, D. D. N., Freeman, H. C., Harvey, I., Lay, P. A., and Bond, A. M. (1996) Voltammetry of plastocyanin at a graphit electrode: Effects of structure, charge, and electrolyte, Inorg. Chem. 35, 7156-7165.
39. Hansen, D. F., Hass, M. A. S., Christensen, H. M., Ulstrup, J., and Led, J. J. (2003) Detection of Short-Lived Transient Protein-Protein Interactions by Intermolecular Nuclear Paramagnetic Relaxation: Plastocyanin from Anabaena variabilis, J. Am. Chem. Soc. 125, 6858-6859.