Abstract
In biological electron transport chains, [2Fe–2S] clusters have versatile electrochemical properties and serve as important electron carriers in a wide variety of biological processes. To understand structural effects on the variation in reduction potentials in [2Fe–2S] proteins, a series of [2Fe–2S] protein analogs with bidentate ligands ( − SC 2 H 4 NH 2) were recently produced by collision-induced dissociation of [Fe 4 S 4(L)4]2− (L = SC 2 H 4 NH 2). Combined with photoelectron spectroscopy findings, the reaction mechanisms of [Fe 4 S 4(L)4]2− to [Fe 2 S 2(L)2]− and the structural effects of ligands on the electronic and redox properties of the [2Fe–2S] clusters are investigated here using broken-symmetry density functional theory method. Our calculations suggest that [Fe 2 S 2(η2 − L)(cis − L)]− and [Fe 2 S 2(η2 − L)2]− are the experimentally observed [2Fe–2S] products, which are generated via a fission process of [Fe 4 S 4(L)4]2− followed by rearrangement of ligands of [Fe 2 S 2(L)2]−. Moreover, structural variation of the ferrous center may dramatically affect the oxidation energy of the [2Fe–2S] clusters.
Similar content being viewed by others
References
Beinert H, Holm RH, Munck E (1997). Science 277:653
Palmer G (1973) Current insight into the active center of spinach ferredoxin and other iron–sulfur proteins. In: Lovenberg W (ed) iron–sulfur protein Academic, vol II. New York, 285
Spiro TG, (ed) (1982) Iron–sulfur proteins, vol IV. Wiley-Interscience, New York
Cammack R (1992). Adv Inorg Chem 38:281
Beinert H (2000). J Biol Inorg Chem 5:2
Wang LS (2001) Clusters. In: Moore JH, Spencer ND (eds) Encyclopedia of chemical physics and physical chemistry, vol III. IOP Publishing, Philadelphia, Vol. III, pp 2113
Bertini I, Ciurli S, Luchinat C (1995) The electronic structure of FeS centers in proteins and models: a contribution to the understanding of their electron transfer properties. In: Clarke MJ, Goodenough JB, Jørgensen CK, Mingos DMP, Neilands JB, Palmer GA, Sadler PJ, Weiss R (eds) structure and bonding, vol 83. Springer, Berlin Heidelberg New York, p 1
Link TA (1999). Adv Inorg Chem 47:83
Leggate EJ, Hirst J (2005). Biochemistry 44:7048
Rose K, Shadle SE, Glaser T, de Vries S, Cherepanov A, Canters GW, Hedman B, Hodgson KO, Solomon EI (1999). J Am Chem Soc 121:2353
Ullmann GM, Noodleman L, Case DA (2002). J Biol Inorg Chem 7:632
Ullmann GM, Noodleman L, Case DA (2001). J Inorg Biochem 86:464
Klingen AR, Ullmann GM (2004). Biochemistry 43:12383
Yang X, Wang XB, Niu S, Pickett CJ, Ichiye T, Wang LS (2002). Phys Rev Lett 89:163401
Niu SQ, Wang XB, Yang X, Wang LS, Ichiye T (2004). J Phys Chem A 108:6750
Fu YJ, Niu S, Ichiye T, Wang LS (2005). Inorg Chem 44:1202
Mouesca JM, Lamotte B (1998). Coord Chem Rev 180:1573
Levine IN (2000) Quantum chemistry, 5th edn. Prentice Hall, Upper Saddle River
Parr RG, Yang W (1989) Density-functional theory of atoms and molecules. Oxford University Press, Oxford
Becke AD (1988). Phys Rev A38:3098
Becke AD (1993). J Chem Phys 98:1372
Becke AD (1993). J Chem Phys 98:5648
Lee C, Yang W, Parr RG (1988). Phys Rev B37:785
Rassolov V, Pople JA, Ratner M, Windus TL (1998). J Chem Phys 109:1223
Francl MM, Petro WJ, Hehre WJ, Binkley JS, Gordon MS, DeFrees DJ, Pople JA (1982). J Chem Phys 77:3654
Hariharan PC, Pople JA (1973). Theor Chim Acta 28:213
Simons J, Joergensen P, Taylor H, Ozment J (1983). J Phys Chem 87:2745
Banerjee A, Adams N, Simons J, Shepard R (1985). J Phys Chem-Us 89:52
Noodleman L, Peng CY, Case DA, Mouesca JM (1995). Coord Chem Rev 144:199
Noodleman L (1981). J Chem Phys 74: 5737
Wang XB, Niu SQ, Yang X, Ibrahim SK, Pickett CJ, Ichiye T, Wang LS (2003). J Am Chem Soc 125:14072
Wang XB, Wang LS (2000). J Chem Phys 112:6959
Niu SQ, Wang XB, Nichols JA, Wang LS, Ichiye T (2003). J Phys Chem A 107:2898
Niu S, Nichols JA, Ichiye T (in preparation)
Yang X, Wang XB, Wang LS, Niu SQ, Ichiye T (2003). J Chem Phys 119:8311
Straatsma TP, Aprà E, Windus TL, Bylaska EJ, de Jong W, Hirata S, Valiev M, Hackler M, Pollack L, Harrison R, Dupuis M, Smith DMA, Nieplocha J, Tipparaju V, Krishnan M, Auer AA, Brown E, Cisneros G, Fann G, Früchtl H, Garza J, Hirao K, Kendall R, Nichols J, Tsemekhman K, Wolinski K, Anchell J, Bernholdt D, Borowski P, Clark T, Clerc D, Dachsel H, Deegan M, Dyall K, Elwood D, Glendening E, Gutowski M, Hess A, Jaffe J, Johnson B, Ju J, Kobayashi R, Kutteh R, Lin Z, Littlefield R, Long X, Meng B, Nakajima T, Niu S, Rosing M, Sandrone G, Stave M, Taylor H, Thomas G, van Lenthe J, Wong A, Zhang Z (2004) NWChem, a computational chemistry package for parallel computers, version 4.6. Pacific Northwest National Laboratory, Richland
Kendall RA, Apra E, Bernholdt DE, Bylaska EJ, Dupuis M, Fann GI, Harrison RJ, Ju JL, Nichols JA, Nieplocha J, Straatsma TP, Windus TL, Wong AT (2000). Comput Phys Commun 128:260
Black G, Didier B, Elsethagen T, Feller D, Gracio D, Hackler M, Havre S,Jones D, Jurrus E, Keller T, Lansing C, Matsumoto S, Palmer B, Peterson M, Schuchardt K, Stephan E, Taylor H, Thomas G, Vorpagel E, Windus T, Winters C (2004) Ecce, a problem solving environment for computational chemistry, software version 321. Pacific Northwest National Laboratory, Richland
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Niu, S., Ichiye, T. Probing the structural effects on the intrinsic electronic and redox properties of [2Fe–2S]+ clusters, a broken-symmetry density functional theory study. Theor Chem Acc 117, 275–281 (2007). https://doi.org/10.1007/s00214-006-0136-y
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00214-006-0136-y