An EPR spin label study of the quinol oxidase, E. coli cytochrome bo 3: A search for redox induced conformational changes

Biochemistry

Volumn 46, Issue 9, 2007, Pages 2355-2363

  White, Gaye F ^a   Field, Sarah ^a   Marritt, Sophie ^a   Oganesyan, Vasily S ^a   Gennis, Robert B ^b   Yap, Lai Lai ^b   Katsonouri, Andromachi ^b,c   Thomson, Andrew J ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c State General Laboratory of Cyprus   (Cyprus)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSOLIC ENTRANCE; QUINOL OXIDASE (QO); REACTION SEQUENCE; SITE DIRECTED NITROXIDE SPIN LABELING (SDSL);

CARBON MONOXIDE; CONFORMATIONS; ENZYMES; ESCHERICHIA COLI; GROWTH KINETICS; REDOX REACTIONS;

PARAMAGNETIC RESONANCE;

CARBON MONOXIDE; COPPER; CYSTEINE; CYTOCHROME; CYTOCHROME BO 3; HEME; NITROXIDE; OXIDOREDUCTASE; OXYGEN; QUINOL OXIDASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CHEMICAL REACTION; CONFORMATIONAL TRANSITION; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; KINETICS; MOTION; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; REACTION ANALYSIS; ROOM TEMPERATURE; SITE DIRECTED NITROXIDE SPIN LABELING; SPIN LABELING;

CRYSTALLOGRAPHY, X-RAY; CYTOCHROMES; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; MODELS, MOLECULAR; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN CONFORMATION; SPIN LABELS;

EID: 33847637098     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi062265h     Document Type: Article

References (33)

1. Brzezinski, P., and Larsson, G. (2003) Redox-driven proton pumping by heme-copper oxidases, Biochim. Biophyx. Acta 1605, 1-13.
2. Namslauer, A., Pawate, A. S., Gennis, R. B., and Brzezinski, P. (2003) Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase, Proc: Natl. Acad. Sci. U.S.A. 100, 15543-15547.
3. Abramson, J., Riistama, S., Larsson, G., Jasaitis, A., Svensson-Ek, M., Laakkonen, L., Puustinen, A., Iwata, S., and Wikstrom, M. (2000) The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site, Nat. Struct. Biol. 7, 910-917.
4. 3 from Escherichia coli, Biochemistry 40, 1077-1082.
5. Grimaldi, S., MacMillan, F., Ostermann, T., Ludwig, B., Michel, H., and Prisner, T. (2001) Ubisemiquinone radical in the bo3-type ubiquinol oxidase studied by pulsed electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy, Biochemistry 40, 1037-1043.
6. 3 is involved in proton translocation. Proc. Natl. Acad. Sci. U.S.A. 94, 10128-10131.
7. 3, Biochemistry 38, 2048-2056.
8. Branden, G., Gennis, R. B., and Brzezinski, P. (2006) Transmem-brane proton translocation by cytochrome c oxidase, Biochim. Biophys. Acta, in press.
9. Hubbell, W. L., Machaourab, H. S., Altenbach, C., and Lietzow, M. A. (1996) Watching proteins move using site-directed spin labelling, Structure 4, 779-793.
10. Hubbell, W. L., Gross, A., Langen, R., and Lietzow, M. A. (1998) Recent advances in site-directed spin labelling of proteins, Curr. Opin. Struct. Biol. 8, 649-656.
11. Hubbell, W. L., Cafiso, D. S., and Altenbach, C. (2000) Identifying conformational changes with site-directed spin labelling, Nat. Struct. Biol. 7, 735-739.
12. Steinhoff, H.-J., Radzwill, N., Thevis, W., Lenz, V., Brandenburg, D., Anston, A., Dodson, G., and Wollmer, A. (1997) Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the x-ray structure, Biophys. J. 73, 3287-3298.
13. Persson, M., Harbridge, J. R., Hammarstrom, P., Mitri, R., Martensson, L.-G., Carlsson, U., Eaton, G. R., and Eaton, S. S. (2001) Comparison of electon paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II, Biophys. J. 80, 2886-2897.
14. Berliner, L. J. (1983) The spin label approach to labelling membrane protein sulfhydryl groups, Ann. N.Y. Acad. Sci. 414, 153-161.
15. Campbell, I. D., and Dwek, R. A. (1984) Electron Paramagnetic Spectroscopy, in Biological Spectroscopy, pp 179-215, Benjamin-Cummings, Menlo Park, CA.
16. Berliner, L. J. (1998) Spin Labeling: The Next Millennium, Biological Magnetic Resonance, Vol. 14. Plenum Press, New York.
17. Columbus, L., and Hubbell, W. L. (2002) A new spin on protein dynamics, Trends Biochem. Sci. 27, 288-295.
18. Barnes, J. P., Liang, Z., Machaourab, H. S., Freed, J. H., and Hubbell, W. L. (1999) A multifrequency electron spin resonance study of T4 Lysozyme dynamics, Biophys. J. 76, 3298-3306.
19. Steinhoff, H.-J., Savitsky, A., Wegener, C., Pfeiffer, M., Plato, M., and Mobius, K. (2000) High-field EPR studies of the structure and conformational changes of site-directed spin labelled bacteriorhodopsin, Biochim. Biophys. Acta 1457, 253-262.
20. Finiguerra, M. G., Van Amsterdam, I. M. C., Alagaratnam. S., Ubbink, M., and Huber, M. (2003) Anisotropic spin label mobilities in azurin from 95 GHz electron paramagnetic resonance Spectroscopy, Chem. Phys. Lett. 382, 528-533.
21. Bennati, M., Gerfen, G. J., Martinez, G. V., Griffiths, R. G., Singel, D. J. and Millhauser, G. L. (1999) Nitroxide side chain dynamics in a spin labelled helix forming peptide revealed by high frequency (139.5 GHz) EPR Spectroscopy, J. Magn. Reson. 139, 281-286.
22. 3 from Escherichia coli and demonstration that associated quinone is not required for structural integrity of the oxidase, Biochim. Biophys. Acla 1340, 131-142.
23. 3: MCD and EPR studies, J. Am. Chem. Soc. 126, 4157-4166.
24. White, G. F., Ottignon, L., Georgiou, T., Kleanthous, C., Moore, G. R., Thomson, A. J., and Oganesyan, V. S. (2007) Analysis of nitroxide spin label motion in a protein-protein complex using multiple frequency EPR Spectroscopy, J. Magn. Reson. 185, 191-203.
25. Robinson, B. H., Slutsky, L. J., and Auteri, F. P. (1992) Direct simulation of continuous wave electron paramagnetic resonance spectra from Brownian dynamics trajectories. J. Chem. Phys. 96, 2609-2616.
26. Steinhoff, H.-J., and Hubbell, W. L. (1996) Calculation of electron paramagnetic resonance spectra from Brownian dynamics trajectories: application to nitroxide side chains in proteins, Biophys. J. 71, 2201-2212.
27. Radzwill, N., Gerwert, K., and Steinhoff, H.-J. (2001) Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin, Biophys. J. 80, 2856-2866.
28. + channel studied by EPR Spectroscopy, Nat. Struct. Biol. 5, 459-469.
29. Perozo, E., Cortes, D. M., Sompornisut, P., Kioda, K., and Martinac, B. (2002) Open channel structure of MscL and the gating mechanism of mechanosensitive channels, Nature 418, 942-948.
30. Langen, R., Oh, K. J., Cascio, D., and Hubbell, W. L. (2000) Crystal structures of spin labeled T4 Lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure. Biochemistry 39, 8396-8405.
31. Busenlehner, L. S., Salomonsson, L., Brzezinski, P., and Armstrong, R. N. (2006) Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase, PNAS 103, 15398-15403.
32. Yoshikawa, S., Shinazawa-Itoh, K., Nakashima, R., Yaono, R., Yamashita, E., Inoue, N., Yao, M., Fei, M. J., Libeu, C. P., Mizushima, T., Yamaguchi, H., Tomizaki, T., and Tsukihara, T. (1998) Redox-coupled, crystal structural changes in bovine heart cytochrome c oxidase, Science 280, 1723-1729.
33. Harrenga, A., and Michel, H. (1999) The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction, J. Biol. Chem. 274, 33296-33299.