A conformational study of the GTPase domain of [FeFe]-hydrogenase maturation protein HydF by PELDOR spectroscopy
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- 作者：Lorenzo Maso (1)
Laura Galazzo (2)
Francesca Vallese (3)
Marilena Di Valentin (2)
Marco Albertini (2)
Edith De Rosa (1)
Giorgio M. Giacometti (1)
Paola Costantini (1)
Donatella Carbonera (2)
1. Department of Biology ; University of Padova ; Viale G. Colombo 3 ; 35131 ; Padua ; Italy
2. Department of Chemical Sciences ; University of Padova ; Via F. Marzolo 1 ; 35131 ; Padua ; Italy
3. Department of Biomedical Sciences ; University of Padova ; Viale G. G. Colombo 3 ; 35131 ; Padua ; Italy - 刊名：Applied Magnetic Resonance
- 出版年：2015
- 出版时间：April 2015
- 年：2015
- 卷：46
- 期：4
- 页码：465-479
- 全文大小：889 KB
- 参考文献：1. Vignais, PM, Billoud, B (2007) Chem. Rev. 107: pp. 4206-4272 g/10.1021/cr050196r" target="_blank" title="It opens in new window">CrossRef
2. Peters, JW, Lanzilotta, WN, Lemon, BJ, Seefeldt, LC (1998) Science 282: pp. 1853-1858 g/10.1126/science.282.5395.1853" target="_blank" title="It opens in new window">CrossRef
3. Nicolet, Y, Piras, C, Legrand, P, Hatchikian, CE, Fontecilla-Camps, JC (1999) Structure 7: pp. 13-23 g/10.1016/S0969-2126(99)80005-7" target="_blank" title="It opens in new window">CrossRef
4. Lubitz, W, Ogata, H, R眉diger, O, Reijerse, E (2014) Chem. Rev. 114: pp. 4081-4148 g/10.1021/cr4005814" target="_blank" title="It opens in new window">CrossRef
5. Shepard, EM, Mus, F, Betz, JN, Byer, AS, Duffus, BR, Peters, JW, Broderick, JB (2014) Biochemistry 53: pp. 4090-4104 g/10.1021/bi500210x" target="_blank" title="It opens in new window">CrossRef
6. Peters, JW, Broderick, JB (2012) Annu. Rev. Biochem. 81: pp. 429-450 g/10.1146/annurev-biochem-052610-094911" target="_blank" title="It opens in new window">CrossRef
7. Posewitz, MC, King, PW, Smolinski, SL, Zhang, L, Seibert, M, Ghirardi, ML (2004) J. Biol. Chem. 279: pp. 25711-25720 g/10.1074/jbc.M403206200" target="_blank" title="It opens in new window">CrossRef
8. Ruback, JK, Brazzolotto, X, Gaillard, J, Fontecave, M (2005) FEBS Lett. 579: pp. 5055-5060 g/10.1016/j.febslet.2005.07.092" target="_blank" title="It opens in new window">CrossRef
9. Brazzolotto, X, Rubach, JK, Gaillard, J, Gambarelli, S, Atta, M, Fontecave, M (2006) J. Biol. Chem. 281: pp. 769-774 g/10.1074/jbc.M510310200" target="_blank" title="It opens in new window">CrossRef
10. McGlynn, SE, Shepard, EM, Winslow, MA, Naumov, AV, Duschene, KS, Posewitz, MC, Broderick, WE, Broderick, JB, Peters, JW (2008) FEBS Lett. 582: pp. 2183-2187 g/10.1016/j.febslet.2008.04.063" target="_blank" title="It opens in new window">CrossRef
11. Mulder, DW, Boyd, ES, Sarma, R, Lange, RK, Endrizzi, JA, Broderick, JB, Peters, JW (2010) Nature 465: pp. 248-251 g/10.1038/nature08993" target="_blank" title="It opens in new window">CrossRef
12. Czech, I, Stripp, S, Sanganas, O, Leidel, N, Happe, T, Haumann, M (2011) FEBS Lett. 585: pp. 225-230 g/10.1016/j.febslet.2010.11.052" target="_blank" title="It opens in new window">CrossRef
13. Berggren, G, Adamska, A, Lambertz, C, Simmons, TR, Esselborn, J, Atta, M, Gambarelli, S, Mouesca, JM, Reijerse, E, Lubitz, W, Happe, T, Artero, V, Fontecave, M (2013) Nature 499: pp. 66-69 g/10.1038/nature12239" target="_blank" title="It opens in new window">CrossRef
14. Esselborn, J, Lambertz, C, Adamska-Venkatesh, A, Simmons, T, Berggren, G, Noth, J, Siebel, J, Hemschemeier, A, Artero, V, Reijerse, E, Fontecave, M, Lubitz, W, Happe, T (2013) Nat. Chem. Biol. 9: pp. 607-609 g/10.1038/nchembio.1311" target="_blank" title="It opens in new window">CrossRef
15. Kuchenreuther, JM, Myers, WK, Suess, DLM, Stich, TA, Pelmenschikov, V, Shiigi, SA, Cramer, SP, Swartz, JR, Britt, RD, George, SJ (2014) Science 343: pp. 424-427 g/10.1126/science.1246572" target="_blank" title="It opens in new window">CrossRef
16. Lawrence, JD, Li, HX, Rauchfuss, TB, Benard, M, Rohmer, MM (2001) Angew. Chem. Int. Ed. 40: pp. 1768-1771 g/10.1002/1521-3773(20010504)40:9<1768::AID-ANIE17680>3.0.CO;2-E" target="_blank" title="It opens in new window">CrossRef
17. King, PW, Posewitz, MC, Ghirardi, ML, Seibert, M (2006) J. Bacteriol. 188: pp. 2163-2172 g/10.1128/JB.188.6.2163-2172.2006" target="_blank" title="It opens in new window">CrossRef
18. Cendron, L, Berto, P, D鈥橝damo, S, Vallese, F, Govoni, C, Posewitz, MC, Giacometti, GM, Costantini, P, Zanotti, G (2011) J. Biol. Chem. 286: pp. 43944-43950 g/10.1074/jbc.M111.281956" target="_blank" title="It opens in new window">CrossRef
19. Berto, P, Valentin, M, Cendron, L, Vallese, F, Albertini, M, Salvadori, E, Giacometti, GM, Carbonera, D, Costantini, P (2012) BBA-Bioenergetics 1817: pp. 2149-2157 g/10.1016/j.bbabio.2012.09.004" target="_blank" title="It opens in new window">CrossRef
20. Shepard, EM, McGlynn, SE, Bueling, AL, Grady-Smith, CS, George, SJ, Winslow, MA, Cramer, SP, Peters, JW, Broderick, JB (2010) Proc. Natl. Acad. Sci. USA 107: pp. 10448-10453 g/10.1073/pnas.1001937107" target="_blank" title="It opens in new window">CrossRef
21. Vallese, F, Berto, P, Ruzzene, M, Cendron, L, Sarno, S, Rosa, E, Giacometti, GM, Costantini, P (2012) J. Biol. Chem. 287: pp. 36544-36555 g/10.1074/jbc.M112.388900" target="_blank" title="It opens in new window">CrossRef
22. Scrima, A, Wittinghofer, A (2006) EMBO J. 25: pp. 2940-2951 g/10.1038/sj.emboj.7601171" target="_blank" title="It opens in new window">CrossRef
23. Ryle, MJ, Lanzilotta, WN, Seefeldt, LC (1996) Biochemistry 35: pp. 9424-9434 g/10.1021/bi9608572" target="_blank" title="It opens in new window">CrossRef
24. Jang, SB, Jeong, MS, Seefeldt, LC, Peters, JW (2004) J. Biol. Inorg. Chem. 9: pp. 1028-1033 g/10.1007/s00775-004-0605-5" target="_blank" title="It opens in new window">CrossRef
25. Chiu, HJ, Peters, JW, Lanzilotta, WN, Ryle, MJ, Seefeldt, LC, Howard, JB, Rees, DC (2001) Biochemistry 40: pp. 641-650 g/10.1021/bi001645e" target="_blank" title="It opens in new window">CrossRef
26. G. Jeschke, M. Pannier, H.W. Spiess, in / Distance Measurements in Biological Systems, vol. 19, ed. by L.J. Berliner, S.S. Eaton, G.R. Eaton (Kluwer Academic, New York, 2000), pp. 493鈥?12
27. Schiemann, O, Prisner, TF (2007) Quart. Rev. Biophys. 40: pp. 1 g/10.1017/S003358350700460X" target="_blank" title="It opens in new window">CrossRef
28. Tsvetkov, YD, Milov, AD, Maryasov, AG (2008) Russ. Chem. Rev. 77: pp. 487 g/10.1070/RC2008v077n06ABEH003782" target="_blank" title="It opens in new window">CrossRef
29. Jeschke, G (2012) Annu. Rev. Phys. Chem. 63: pp. 419 g/10.1146/annurev-physchem-032511-143716" target="_blank" title="It opens in new window">CrossRef
30. Stoll, S, Schweiger, A (2006) J. Magn. Reson. 178: pp. 42-55 g/10.1016/j.jmr.2005.08.013" target="_blank" title="It opens in new window">CrossRef
31. Polyhach, Y, Bordignon, E, Jeschke, G (2010) Phys. Chem. Chem. Phys. 13: pp. 2356-2366 g/10.1039/C0CP01865A" target="_blank" title="It opens in new window">CrossRef
32. Jeschke, G, Chechik, V, Ionita, P, Godt, A, Zimmermann, H, Banham, J, Timmel, CR, Hilger, D, Jung, H (2006) Appl. Magn. Reson. 30: pp. 473-498 g/10.1007/BF03166213" target="_blank" title="It opens in new window">CrossRef - 刊物类别：Chemistry and Materials Science
- 刊物主题：Chemistry
Analytical Chemistry - 出版者：Springer Wien
- ISSN：1613-7507
文摘
[FeFe]-hydrogenases catalyze the reversible interconversion of protons to molecular hydrogen (H2) at an active site called H-cluster. The maturation pathway of these enzymes is a complex process involving three proteins, HydE, HydF and HydG. The maturase protein HydF has been suggested to interact with HydE and HydG and to be the transferase that shuttles the complete H-cluster to the hydrogenase; however, the exact molecular mechanism driving this translocation remains unclear. HydF is constituted by three different domains: a N-terminal GTP-binding domain, a dimerization domain and a C-terminal [4Fe4S] cluster-binding domain. To investigate possible conformational changes induced by the GTP binding in the N-terminal domain, we have expressed, in Escherichia coli, a recombinant HydF protein from Thermotoga neapolitana including the GTP-binding domain only. Site-directed mutants were designed in which the native residues were substituted by cysteines and subsequently spin labeled with the nitroxide MTSSL. CW-EPR was used to study the local mobility of the nitroxides at each site, and double spin-labeled mutants have been investigated by PELDOR spectroscopy. We found that the binding of the nucleotide does not induce large conformational effects within the isolated GTP domain, at least at the level of the elements investigated in this work. However, small changes in the distance between spin labels were observed which might reflect diffuse structural rearrangements. We suggest that the variations following the GTP binding could affect the dimer form adopted by the whole HydF protein in solution and, as a consequence, the interactions with the other maturases.