Biological iron-sulfur clusters: Mechanistic insights from mass spectrometry

Coordination Chemistry Reviews - Tập 448 - Trang 214171 - 2021
Jason C. Crack1, Nick E. Le Brun1
1School of Chemistry, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK

Tài liệu tham khảo

Maret, 2018, Adv. Exp. Med. Biol., 1055, 1, 10.1007/978-3-319-90143-5_1 Hagedoorn, 2015, Proteomes, 3, 424, 10.3390/proteomes3040424 Howard, 1991, Adv. Protein Chem., 42, 199, 10.1016/S0065-3233(08)60537-9 Reedy, 2004, Chem. Rev., 104, 617, 10.1021/cr0206115 Zanello, 2017, J. Struct. Biol., 200, 1, 10.1016/j.jsb.2017.05.010 Zanello, 2018, J. Struct. Biol., 202, 250, 10.1016/j.jsb.2018.01.010 Zanello, 2018, J. Struct. Biol., 202, 264, 10.1016/j.jsb.2018.03.008 Zanello, 2019, J. Struct. Biol., 205, 103, 10.1016/j.jsb.2019.01.003 Johnson, 1998, Curr. Opin. Chem. Biol., 2, 173, 10.1016/S1367-5931(98)80058-6 Beinert, 1997, Science, 277, 653, 10.1126/science.277.5326.653 Bailey, 2011, Nat. Chem. Biol., 8, 24, 10.1038/nchembio.737 Bian, 1999, Coord Chem Revs, 190–192, 1049, 10.1016/S0010-8545(99)00157-5 Broderick, 2019, J. Biol. Inorg. Chem., 24, 769, 10.1007/s00775-019-01706-w Werth, 1992, FEBS Lett., 299, 1, 10.1016/0014-5793(92)80086-V Volbeda, 2019, J. Am. Chem. Soc., 141, 2367, 10.1021/jacs.8b10823 Fleischhacker, 2012, Biochemistry, 51, 4453, 10.1021/bi3003204 Hernandez, 2008, Proc. Natl. Acad. Sci. U S A, 105, 11679, 10.1073/pnas.0803576105 Shomura, 2011, Nature, 479, 253, 10.1038/nature10504 Noodleman, 1995, Coord. Chem. Rev., 144, 199, 10.1016/0010-8545(95)07011-L Mouesca, 1995, Inorg. Chem., 34, 4347, 10.1021/ic00121a013 Imlay, 2006, Mol. Microbiol., 59, 1073, 10.1111/j.1365-2958.2006.05028.x Guo, 2017, 77 Hagen, 2018, J. Biol. Inorg. Chem., 23, 623, 10.1007/s00775-018-1543-y Petasis, 2017, 135 Chakrabarti, 2017, 163 Pandelia, 2015, BBA, 1853, 1395 Todorovic, 2018, J. Biol. Inorg. Chem., 23, 647, 10.1007/s00775-018-1533-0 Volbeda, 2015, Sci. Adv., 1, 10.1126/sciadv.1501086 Cai, 2018, Molecules, 23, 2213, 10.3390/molecules23092213 Maiocco, 2018, Methods Enzymol., 606, 319, 10.1016/bs.mie.2018.06.002 Thomson, 1991, Biochem. Soc. Trans., 19, 594, 10.1042/bst0190594 Noodleman, 2017, 21 Noodleman, 2002, Curr. Opin. Chem. Biol., 6, 259, 10.1016/S1367-5931(02)00309-5 Crack, 2020, J. Am. Chem. Soc., 142, 5104, 10.1021/jacs.9b12250 Katta, 1991, J. Am. Chem. Soc., 113, 8534, 10.1021/ja00022a058 Moulis, 1993, Arch. Biochem. Biophys., 305, 186, 10.1006/abbi.1993.1409 Hu, 1995, J. Mass Spectrom., 30, 1076, 10.1002/jms.1190300803 Zaia, 1998, Protein Sci., 7, 2398, 10.1002/pro.5560071117 Gumerov, 2001, Anal. Chem., 73, 2565, 10.1021/ac0015164 Loo, 1997, Mass Spectrom. Rev., 16, 1, 10.1002/(SICI)1098-2787(1997)16:1<1::AID-MAS1>3.0.CO;2-L Chandler, 2018, Curr. Opin. Chem. Biol., 42, 130, 10.1016/j.cbpa.2017.11.019 Leney, 2017, J. Am. Soc. Mass Spectrom., 28, 5, 10.1007/s13361-016-1545-3 Heck, 2008, Nat. Methods, 5, 927, 10.1038/nmeth.1265 Leszczyszyn, 2010, PCCP, 12, 13408, 10.1039/c0cp00680g Perez-Rafael, 2011, Talanta, 83, 1057, 10.1016/j.talanta.2010.10.060 Ross, 2020, Chem. Commun., 56, 3417, 10.1039/C9CC08130E Scheller, 2018, Dalton Trans., 47, 3613, 10.1039/C7DT03319B Ott, 2019, Metallomics, 11, 968, 10.1039/c8mt00308d Lermyte, 2019, J. Am. Soc. Mass Spectrom., 30, 2123, 10.1007/s13361-019-02283-7 Maniero, 2020, J. Trace Elem. Med Biol., 58, 10.1016/j.jtemb.2019.126441 Hare, 2016, Meth Mol Biol, 1303, 379, 10.1007/978-1-4939-2627-5_22 Puglisi, 2020, FEBS J., 287, 2428, 10.1111/febs.15281 Lin, 2020, J. Am. Chem. Soc., 142, 6018, 10.1021/jacs.9b11454 Jia, 2020, Angew. Chem. Int. Ed., 59, 6724, 10.1002/anie.201915615 Gervason, 2019, Nat. Commun., 10, 3566, 10.1038/s41467-019-11470-9 Woodall, 2020, Anal. Chem., 92, 3440, 10.1021/acs.analchem.9b05561 Kay, 2019, J. Inorg. Biochem., 190, 24, 10.1016/j.jinorgbio.2018.10.004 Zhou, 2018, Biochim Biophys Acta Proteins Proteom, 1866, 275, 10.1016/j.bbapap.2017.11.008 Bennett, 2019, Chem. Sci., 10, 4985, 10.1039/C9SC01053J Blindauer, 2003, J. Am. Chem. Soc., 125, 3226, 10.1021/ja0284409 J.C. Crack, N.E. Le Brun, in: J.M. Walker (Ed.) Meth Mol Biol, Nature-Springer, 2021. ISBN 978-1-0716-1604-8 Kondrat, 2013, Chem. Commun., 49, 813, 10.1039/C2CC38387J Kaltashov, 2018, Methods, 144, 14, 10.1016/j.ymeth.2018.04.019 Bich, 2010, J. Am. Soc. Mass Spectrom., 21, 286, 10.1016/j.jasms.2009.10.012 Heck, 2004, Mass Spectrom. Rev., 23, 368, 10.1002/mas.10081 Sobott, 2005, Phil Trans A, Math Phys, Eng. Sci., 363, 379 Johnson, 2000, Anal. Chem., 72, 1410, 10.1021/ac991183e Crack, 2017, Proc. Natl. Acad. Sci. U S A, 114, E3215, 10.1073/pnas.1620987114 Hagen, 1981, J. Am. Chem. Soc., 103, 4054, 10.1021/ja00404a013 Freibert, 2018, Meth Enzymol, 599, 197, 10.1016/bs.mie.2017.11.034 Braymer, 2021, Biochim. Biophys. Acta, Mol. Cell. Res., 1868, 10.1016/j.bbamcr.2020.118863 Blanc, 2015, BBA, 1853, 1436 Tsaousis, 2019, Front. Microbiol., 10, 2478, 10.3389/fmicb.2019.02478 Mettert, 2015, Annu. Rev. Microbiol., 69, 505, 10.1146/annurev-micro-091014-104457 Shi, 2010, PLoS Biol., 8 Kim, 2012, Biochemistry, 51, 5557, 10.1021/bi300579p Shimomura, 2008, J. Mol. Biol., 383, 133, 10.1016/j.jmb.2008.08.015 Marinoni, 2012, Angew. Chem. Int. Ed., 51, 5439, 10.1002/anie.201201708 Sato, 2020, Mol. Microbiol. Kim, 2009, Biochemistry, 48, 6062, 10.1021/bi9002277 Markley, 2013, FEBS Lett., 587, 1172, 10.1016/j.febslet.2013.01.003 Nuth, 2002, J. Am. Chem. Soc., 124, 8774, 10.1021/ja0264596 Lewis, 2019, Metallomics, 11, 1820, 10.1039/C9MT00172G Rodrigues, 2015, Biometals, 28, 567, 10.1007/s10534-015-9846-8 Keyer, 1996, Proc. Natl. Acad. Sci. U S A, 93, 13635, 10.1073/pnas.93.24.13635 Ramelot, 2004, J. Mol. Biol., 344, 567, 10.1016/j.jmb.2004.08.038 Li, 2019, Appl. Environ. Microbiol., 85, e01967 Outten, 2001, Science, 292, 2488, 10.1126/science.1060331 Adinolfi, 2017, Front Mol Biosci, 4, 97, 10.3389/fmolb.2017.00097 Rajagopalan, 2013, Nat. Struct. Mol. Biol., 20, 740, 10.1038/nsmb.2568 Crack, 2020, Encyclopedia of Inorganic and Bioinorganic Chemistry, Wiley, 1 Johnston, 2007, Biometals, 20, 501, 10.1007/s10534-007-9085-8 Pellicer Martinez, 2017, Chem. Sci., 8, 8451, 10.1039/C7SC02801F Todd, 2005, Mol. Genet. Genomics, 273, 197, 10.1007/s00438-005-1127-8 Todd, 2002, Microbiology, 148, 4059, 10.1099/00221287-148-12-4059 Singleton, 2010, J. Biol. Chem., 285, 16023, 10.1074/jbc.M109.067215 Behringer, 2020, Biochem. J., 477, 191, 10.1042/BCJ20180734 Volbeda, 2017, Nat. Commun., 8, 15052, 10.1038/ncomms15052 Pellicer Martinez, 2019, Elife, 8, 10.7554/eLife.47804 Kuzmic, 2009, Meth Enzymol, 467, 247, 10.1016/S0076-6879(09)67010-5 Crack, 2019, Biol Meth Prot, 4, byp015, 10.1093/biomethods/bpy015 Crack, 2014, Meth Mol Biol, 1122, 33, 10.1007/978-1-62703-794-5_4 Beaumont, 2004, Mol. Microbiol., 54, 148, 10.1111/j.1365-2958.2004.04248.x Partridge, 2009, Mol. Microbiol., 73, 680, 10.1111/j.1365-2958.2009.06799.x Crack, 2018, Chem. Commun., 54, 5992, 10.1039/C8CC01339J Crack, 2016, J. Biol. Chem., 291, 8663, 10.1074/jbc.M115.693192 Crack, 2015, J. Biol. Chem., 290, 12689, 10.1074/jbc.M115.643072 Tucker, 2008, PLoS ONE, 3, 10.1371/journal.pone.0003623 Crack, 2019, Chemistry, 25, 3675, 10.1002/chem.201806113 Tucker, 2010, Trends Microbiol., 18, 149, 10.1016/j.tim.2009.12.009 Butler, 1988, Inorg. Chem., 32, 335 Butler, 2002, Chem. Rev., 102, 1155, 10.1021/cr000076d Crack, 2014, Acc. Chem. Res., 47, 3196, 10.1021/ar5002507 Serrano, 2016, Angew. Chem. Int. Ed., 55, 14575, 10.1002/anie.201607033 Lewandowska, 2011, Dalton Trans., 40, 8273, 10.1039/c0dt01244k Crack, 2011, J. Am. Chem. Soc., 133, 1112, 10.1021/ja109581t Tonzetich, 2010, J. Am. Chem. Soc., 132, 6914, 10.1021/ja101002f Grabarczyk, 2019, Dalton Trans., 48, 13960, 10.1039/C9DT00924H Keefer, 1996, Meth Enzymol, 268, 281, 10.1016/S0076-6879(96)68030-6 Rivera-Tirado, 2011, Rapid Commun. Mass Spectrom., 25, 3581, 10.1002/rcm.5273 A. Volbeda, Y. Nicolet, J.C. Fontecilla-Camps, Fumarate and Nitrate Reduction Regulator (FNR), in: Encyclopedia of Inorganic and Bioinorganic Chemistry, pp. 1-11. Lazazzera, 1993, Genes Dev., 7, 1993, 10.1101/gad.7.10.1993 Lazazzera, 1996, J. Biol. Chem., 271, 2762, 10.1074/jbc.271.5.2762 Khoroshilova, 1995, Proc. Natl. Acad. Sci. U S A, 92, 2499, 10.1073/pnas.92.7.2499 Green, 1996, Biochem. J., 316, 887, 10.1042/bj3160887 Crack, 2004, J. Biol. Chem., 279, 9278, 10.1074/jbc.M309878200 Khoroshilova, 1997, Proc. Natl. Acad. Sci. U S A, 94, 6087, 10.1073/pnas.94.12.6087 Crack, 2008, J. Am. Chem. Soc., 130, 1749, 10.1021/ja077455+ Sutton, 2004, J. Bacteriol., 186, 8018, 10.1128/JB.186.23.8018-8025.2004 Lamberg, 2002, J. Mol. Biol., 315, 275, 10.1006/jmbi.2001.5241 Popescu, 1998, Proc. Natl. Acad. Sci. U S A, 95, 13431, 10.1073/pnas.95.23.13431 Crack, 2007, Proc. Natl. Acad. Sci. U S A, 104, 2092, 10.1073/pnas.0609514104 Crack, 2006, J. Biol. Chem., 281, 18909, 10.1074/jbc.C600042200 Zhang, 2012, Proc. Natl. Acad. Sci. U S A, 109, 15734, 10.1073/pnas.1208787109 Mettert, 2018, Antioxid. Redox Signal., 29, 1830, 10.1089/ars.2017.7365 Jervis, 2009, Proc. Natl. Acad. Sci. USA, 106, 4659, 10.1073/pnas.0804943106 Johnson, 2001, J. Am. Soc. Mass Spectrom., 12, 819, 10.1016/S1044-0305(01)00263-X Attwood, 2004, Anal. Biochem., 334, 382, 10.1016/j.ab.2004.08.010 Irvine, 2015, Chemistry, 21, 1269, 10.1002/chem.201404283 Fritsch, 2011, Nature, 479, 249, 10.1038/nature10505 Lee, 2016, Chem. Commun., 52, 1174, 10.1039/C5CC07813J Pettersen, 2004, J. Comp. Chem., 25, 1605, 10.1002/jcc.20084