Abstract
A subset of the large family of nonheme iron oxygenases carries out the oxidative decarboxylation of α-ketocarboxylate and α-hydroxycarboxylate substrates in the presence of O2. Iron complexes of α-ketocarboxylates and α-hydroxycarboxylates supported by tridentate and tetradentate ligands have been synthesized to act as functional models for these enzymes, and several have been structurally characterized. From studies of these model complexes and their reactivity toward various probe substrates, insights into the reaction mechanisms have been obtained, where iron(III)-superoxo and iron(IV)-oxo species have been implicated as key oxidants.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Hausinger RP (2004) Crit Rev Biochem Mol Biol 39:21–68
Koehntop KD, Emerson JP, Que L Jr (2005) J Biol Inorg Chem 10:87–93
Costas M, Mehn MP, Jensen MP, Que L Jr (2004) Chem Rev 104:939–986
Elkins JM, Ryle MJ, Clifton IJ, Hotopp JCD, Lloyd JS, Burzlaff NI, Baldwin JE, Hausinger RP, Roach PL (2002) Biochemistry 41:5185–5192
Price JC, Barr EW, Hoffart LM, Krebs C, Bollinger JM Jr (2005) Biochemistry 44:8138–8147
Sinnecker S, Svensen N, Barr EW, Ye S, Bollinger JM Jr, Neese F, Krebs C (2007) J Am Chem Soc 129:6168–6179
Price JC, Barr EW, Tirupati B, Bollinger JM Jr, Krebs C (2003) Biochemistry 42:7497–7508
Hoffart LM, Barr EW, Guyer RB, Bollinger JM Jr, Krebs C (2006) Proc Natl Acad Sci USA 103:14738–14743
Galonić DP, Barr EW, Walsh CT, Bollinger JM Jr, Krebs C (2007) Nat Chem Biol 3:113–116
Matthews ML, Krest CM, Barr EW, Vaillancourt FH, Walsh CT, Green MT, Krebs C, Bollinger JM Jr (2009) Biochemistry 48:4331–4343
Krebs C, Fujimori DG, Walsh CT, Bollinger JM Jr (2007) Acc Chem Res 40:484–492
Riggs-Gelasco PJ, Price JC, Guyer RB, Brehm JH, Barr EW, Bollinger JM Jr, Krebs C (2004) J Am Chem Soc 126:8108–8109
Galonić Fujimori DB, Barr EW, Matthews ML, Koch GM, Yonce JR, Walsh CT, Bollinger JM Jr, Krebs C, Riggs-Gelasco PJ (2007) J Am Chem Soc 129:13408–13409
Price JC, Barr EW, Glass TE, Krebs C, Bollinger JM Jr (2003) J Am Chem Soc 125:13008–13009
Pojer F, Kahlich R, Kammerer B, Li S-M, Heide L (2003) J Biol Chem 278:30661–30668
van der Donk W, Krebs C, Bollinger JM Jr (2010) Curr Opin Struct Biol 20:673–683
Chiou Y-M, Que L Jr (1992) J Am Chem Soc 114:7567–7568
Chiou Y-M, Que L Jr (1995) J Am Chem Soc 117:3999–4013
Ho RYN, Mehn MP, Hegg EL, Liu A, Ryle MJ, Hausinger RP, Que L Jr (2001) J Am Chem Soc 123:5022–5029
Pavel EG, Kitajima N, Solomon EI (1998) J Am Chem Soc 120:3949–3962
Hegg EL, Ho RYN, Que L Jr (1999) J Am Chem Soc 121:1972–1973
Hegg EL, Whiting AK, Saari RE, McCracken J, Hausinger RP, Que L Jr (1999) Biochemistry 38:16714–16726
Ryle MJ, Padmakumar R, Hausinger RP (1999) Biochemistry 38:15278–15286
Paine TK, England J, Que L Jr (2007) Chem Eur J 13:6073–6081
Friese SJ, Kucera BE, Young VG Jr, Que L Jr, Tolman WB (2008) Inorg Chem 47:1324–1331
Sheet D, Halder P, Paine TK (2013) Angew Chem Int Ed 52:13314–13318
Paine TK, Zheng H, Que L Jr (2005) Inorg Chem 44:474–476
Di Giuro CML, Buongiorno D, Leitner E, Straganz GD (2011) J Inorg Biochem 105:1204–1211
Allpress CJ, Berreau LM (2013) Coord Chem Rev 257:3005–3029
Burzlaff N (2009) Angew Chem Int Ed 48:5580–5582
Ha EH, Ho RYN, Kisiel JF, Valentine JS (1995) Inorg Chem 34:2265–2266
Hikichi S, Ogihara T, Fujisawa K, Kitajima N, Akita M, Moro-oka Y (1997) Inorg Chem 36:4539–4547
Mehn MP, Fujisawa K, Hegg EL, Que L Jr (2003) J Am Chem Soc 125:7828–7842
Mukherjee A, Cranswick MA, Chakrabarti M, Paine TK, Fujisawa K, Münck E, Que L Jr (2010) Inorg Chem 49:3618–3628
Kitajima N, Osawa M, Tanaka M, Moro-oka Y (1991) J Am Chem Soc 113:8952–8953
Reinaud OM, Theopold KH (1994) J Am Chem Soc 116:6979–6980
Kitajima N, Tamura N, Amagai H, Fukui H, Moro-oka Y, Mizutani Y, Kitagawa T, Mathur R, Heerwegh K, Reed CA, Randall CR, Que L Jr, Tatsumi K (1994) J Am Chem Soc 116:9071–9085
Mukherjee A, Martinho M, Bominaar EL, Münck E, Que L Jr (2009) Angew Chem Int Ed 48:1780–1783
Usharani D, Janardanan D, Shaik S (2011) J Am Chem Soc 133:176–179
McDonald AR, Que L Jr (2013) Coord Chem Rev 257:414–428
Paine TK, Paria S, Que L Jr (2010) Chem Commun 46:1830–1832
Paria S, Que L Jr, Paine TK (2011) Angew Chem Int Ed 50:11129–11132
Acknowledgments
The authors are supported respectively by the DST, Govt. of India (Project: SR/S1/IC-51/2010), and the US National Science Foundation (Grant CHE-1058248). We thank Dr. Caleb Allpress for a careful reading of the final manuscript.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2014 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Paine, T.K., Que, L. (2014). Dioxygen Activation by Biomimetic Iron Complexes of α-Keto Acids and α-Hydroxy Acids. In: Rabinovich, D. (eds) Molecular Design in Inorganic Biochemistry. Structure and Bonding, vol 160. Springer, Berlin, Heidelberg. https://doi.org/10.1007/430_2014_144
Download citation
DOI: https://doi.org/10.1007/430_2014_144
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-43598-4
Online ISBN: 978-3-662-43599-1
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)