Abstract
Poly(l-histidine) and imidazole in the presence of copper cations have been investigated by means of Fourier transform infrared (IR) spectroscopy in the mid- and far-IR spectral range to establish specific marker bands of the copper-coordination site in metalloproteins as a function of pH as well as the effect of the coordination on the amino acid contributions. Whereas the well-known mid-IR region was specific for the secondary structure of the protein mimics, the far-IR region included contributions from the metal–ligand vibrations. The addition of copper led to secondary structure changes of poly(l-histidine) at neutral and basic pD and to specific shifts of ring vibrations. At pD 9.5 the addition of copper deprotonated the nitrogen atoms of the imidazole ring and the backbone. At neutral pD the copper cations were coordinated by the N3 atom of the imidazole ring. Copper–imidazole vibrations at neutral pD were observed at 154 and 128 cm−1. Signals observed at 313 and 162 cm−1 were assigned to metal–ligand vibrations arising from copper–poly(l-histidine) complexes with a negatively charged imidazole ring.
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Abbreviations
- FTIR:
-
Fourier transform infrared
- His:
-
Histidine
- Im:
-
Imidazole
- IR:
-
Infrared
- 4-MeIm:
-
4-Methylimidazole
- PLH:
-
Poly(l-histidine)
- υ:
-
Stretching vibration
- δ:
-
Bending vibration
- δdef :
-
Deformation vibration
- γ:
-
Wagging vibration
- τ:
-
Torsion vibration
References
Dörr S, Schade U, Hellwig P, Ortolani M (2007) J Phys Chem B 111:14418–14422
Ebbinghaus S, Kim SJ, Heyden M, Yu X, Gruebele M, Leitner DM, Havenith M (2008) J Am Chem Soc 130:2374–2375
Brubach JB, Mermet A, Filabozzi A, Gerschel A, Roy P (2005) Chem Phys 122:184509–184515
Zelsmann HR (1995) J Mol Struct 350:95–114
Williams PA, Blackburn NJ, Sanders D, Bellamy H, Stura EA, Fee JA, McRee DE (1999) Nat Struct Biol 6:509–516
Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, Than ME (2000) EMBO J 19:1766–1776
Hunsicker-Wang LM, Heine A, Chen Y, Luna EP, Todaro T, Zhang YM, Williams PA, McRee DE, Hirst J, Stout D, Fee JA (2003) Biochemistry 42:7303–7317
Iwata S, Saynovits M, Link TA, Michel H (1996) Structure 4:567–570
Frieden E, Osaki S, Kobayashi H (1965) J Gen Physiol 49:213–252
Beinert H, Holm RH, Münck E (1997) Science 277:653–659
Meyer J (2008) J Biol Inorg Chem 13:157–170
Rees DC (2002) Annu Rev Biochem 71:221–246
Miura T, Satoh T, Hori-i A, Takeuchi H (1998) J Raman Spectrosc 29:41–47
Wang X, Lee JS, Yang DS (2006) J Phys Chem A 110:12777–12784
Mesu JG, Visser T, Soulimani F, Weckhuysen BM (2005) Vib Spectrosc 39:114–125
Mesu JG, Visser T, Soulimani F, Van Faassen EE, De Peinder P, Beale AM, Weckhuysen BM (2006) Inorg Chem 45:1960–1971
Deschamps P, Kulkarni PP, Gautam-Basak M, Sarkar B (2005) Coord Chem Rev 249:895–909
Mesu GJ, Visser T, Beale AM, Soulimani F, Weckhuysen BM (2006) Chem Eur J 12:7167–7177
Bi X, Yang KL (2007) Langmuir 23:11067–11073
Deschamps P, Kulkarni PP, Sarkar B (2004) Inorg Chem 43:3338–3340
Sigel H, McCormick DB (1971) J Am Chem Soc 93:2041–2044
Torreggiani A, Tamba M, Bonora S, Fini G (2003) Biopolymers 72:290–298
Drożdżewski P, Kordon E (2000) Spectrochim Acta A Mol Biomol Spectrosc 56:1299–1304
Cheruzel LE, Cecil MR, Edison SE, Mashuta MS, Baldwin MJ, Buchanan RB (2006) Inorg Chem 45:3191–3202
Jakab NI, Gyurcsik B, Körtvélyesi T, Vosekalna I, Jensen J, Larsen E (2007) J Inorg Biochem 101:1376–1385
Kállay C, Várnagy K, Malandrinos G, Hadjiliadis N, Sanna D, Sόvágό I (2006) Dalton Trans 4545–4552
White KN, Sen I, Szundi I, Landaverry YR, Bira LE, Konopelski JP, Olmstead MM, Einarsdόttir Ó (2007) Chem Commun 3252–3254
Materazzi S, Kurdziel K, Tentolini U, Bacaloni A, Aquili S (2003) Thermochim Acta 395:133–137
Materazzi S, D’Ascenzo G, Aquili S, Kadish KM, Bear JL (2003) Thermochim Acta 397:129–134
Liang HC, Dahan M, Karlin KD (1999) Curr Opin Chem Biol 3:168–175
Inoue T, Sugawara H, Hamanaka S, Tsukui H, Suzuki E, Kohzuma T, Kai Y (1999) Biochemistry 38:6063–6069
Ellis MJ, Dodd FE, Strange RW, Prudêncio M, Sawers G, Eady RR, Hasnain SS (2001) Acta Crystallogr D Biol Crystallogr D57:1110–1118
Zhang L, Koay M, Maher MJ, Xiao Z, Wedd AG (2006) J Am Chem Soc 128:5834–5850
Hough MA, Hasnain SS (2003) Structure 11:937–946
Colbert CL, Couture M, Eltis LD, Bolin JT (2000) Structure 8:1267–1278
Kolling DJ, Brunzelle JS, Lhee SM, Crofts AR, Nair SK (2007) Structure 15:29–38
Gao X, Wen X, Esser L, Quinn B, Yu L, Yu CA, Xia D (2003) Biochemistry 42:9067–9080
Iwaki M, Yakovlev G, Hirst J, Osyczka A, Dutton PL, Marshall D, Rich PR (2005) Biochemistry 44:4230–4237
Loeffen PW, Pettifer RF, Fillaux F, Kearley GJ (1995) J Chem Phys 103:8444–8455
Hasegawa K, Ono TA, Noguchi T (2000) J Phys Chem B 104:4253–4265
Hasegawa K, Ono TA, Noguchi T (2002) J Phys Chem A 106:3377–3390
Pecht I, Levitzki A, Anbar M (1967) J Am Chem Soc 89:1587–1591
Levitzki A, Pecht I, Berger A (1972) J Am Chem Soc 94:6844–6849
Dovbeshko G, Berezhinsky L (1998) J Mol Struct 450:121–128
Xie A, He Q, Miller L, Sclavi B, Chance MR (1999) Biopolymers 49:591–603
Maklakov LI, Aksakova SV (1997) Russ Chem Rev 66:375–388
Berthomieu C, Marboutin L, Dupeyrat F, Bouyer P (2006) Biopolymers 82:363–367
Dörr S, Hellwig P (2008) Vib Spectrosc 47:59–65
Chu HA, Gardner MT, Hillier W, Babcock GT (2000) Photosynth Res 66:57–63
Kowalik-Jankowska T, Ruta M, Wiśniewska K, Łankiewicz L (2003) J Inorg Chem 95:270–282
Kállay C, Nagy Z, Várnagy K, Malandrinos G, Hadjiliadis N, Sόvágό I (2007) Bioinorg Chem Appl 30394
Barth A (2000) Prog Biophys Mol Biol 74:141–173
Muehlinghaus J, Zundel G (1971) Biopolymers 10:711–719
Kong J, Yu S (2007) Acta Biochim Biophys Sin 39:549–559
Dong A, Huang P, Caughey WS (1990) Biochemistry 29:3303–3308
He WZ, Newell WR, Haris PI, Chapman D, Barber J (1991) Biochemistry 30:4552–4559
Kalnin NN, Baikalov IA, Venyaminov SY (1990) Biopolymers 30:1273–1280
Miyazawa T, Shimanouchi T, Mizushima SI (1958) J Chem Phys 29:611–616
Jung C (2000) Mol Recogn 13:325–351
Wolpert M, Hellwig P (2006) Spectrochim Acta A Mol Biomol Spectrosc 64:987–1001
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Financial support by the ANR (agence nationale de recherche), the CNRS, and the French ministry for research is gratefully acknowledged.
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El Khoury, Y., Hellwig, P. Infrared spectroscopic characterization of copper–polyhistidine from 1,800 to 50 cm−1: model systems for copper coordination. J Biol Inorg Chem 14, 23–34 (2009). https://doi.org/10.1007/s00775-008-0421-4
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DOI: https://doi.org/10.1007/s00775-008-0421-4