Abstract
Recent developments in zinc enzyme models, in particular for carbonic anhydrase (CA), alkaline phosphatase (AP), and alcohol dehydrogenase (ADH) are presented. Although these models are simple zinc(II) complexes, they have helped to disclose the hitherto unsettled intrinsic properties of zinc (II)-dependent enzyme functions. The discussion emphasizes how H2O is activated by zinc(II) for the nucleophilic attack on electrophilic substrates (e.g., CO2 in CA, phosphomonoesters in AP) and also how alcohols are activated by zinc (II) for hydride transfer in ADH or nucleophilic attack on phosphates in AP. Future modeling should take into consideration the results from recent developments in enzyme functions by protein engineering. For instance, design of secondary zinc(II) ligands for the fine-tuning of zinc(II) properties will be needed to explore and understand the reaction specificity of zinc enzymes.
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Kimura E, Koike T (1996) In: Comprehensive Supramolecular Chemistry, Vol 10:429, Pergamon
Kimura E (1994) Prog Inorg Chem 41:443
Kimura E, Shionoya M (1994) in Transition Metals in Supramolecular Chemistry, 245, John Wiley
Kimura E, Koike T (1991) Comments Inorg Chem 11:285
Kimura E, Shiota T, Koike T, Shiro M, Kodama M (1990) J Am Chem Soc 112:5805
Koike T, Kimura E (1991) J Am Chem Soc 113:8935
Zhang X, von Eldic R, Koike T, Kimura E (1993) Inorg Chem 32:5749
Kimura E, Koike T, Shionoya M, Shiro M (1992) Chem Lett 787
Koike T, Kimura E, Nakamura I, Hashimoto Y, Shiro M (1992) J Am Chem Soc 114:7338
Kimura E, Nakamura I, Koike T, Shionoya M, Kodama Y, Ikeda T, Shiro M (1994) J Am Chem Soc 116:4764
Koike T, Takamura M, Kimura E (1994) J Am Chem Soc 116:8443
Koike T, Kajitani S, Nakamura I, Kimura E, Shiro M (1995) J Am Chem Soc 117:1210
Kimura E, Kodama Y, Koike T, Shiro M (1995) J Am Chem Soc 117:8304
Zhang X, von Eldik R (1995) Inorg Chem 34:5606
Read RJ, James MN (1981) J Am Chem Soc 103:6947
Brown RS, Curtis NJ, Huguet J (1981) J Am Chem Soc 103:6953
Brown RS, Salmon D, Curtis NJ, Kusuma S (1982) J Am Chem Soc 104:3188
Slebocka-Tilk H, Cocho JL, Frakman Z, Brown RS (1984) J Am Chem Soc 106:2421
Alsfasser R, Trofimenko S, Looney A, Parkin G, Vahrenkamp H (1991) Inorg Chem 30:4098
Looney A, Han R, McNeill K, Parkin G (1993) J Am Chem Soc 115:4690
Looney A, Parkin G (1994) Inorg Chem 33:1234
Kitajima N, Hikichi S, Tanaka M, Moro-oka Y (1993) J Am Chem Soc 115:5496
Woolley P (1975) Nature, 258:677
Botrè F, Gros G, Storey BT (1991) Carbonic anhydrase. VCH, Weinheim
Khalifah RG (1971) J Biol Chem 246:2561
Nair SK, Calderone TL, Christianson DW Fierker CA (1991) J Biol Chem 266:17320
Palmer DA, von Erdic R (1983) Chem Rev 83:651
Mahal G, von Erdic R (1985) Inorg Chem 24:4165
Ruf M, Weis K, Vahrenkamp H (1994) J Chem Soc Chem Commun 135
Murthy NN, Karlin KD (1993) J Chem Soc Chem Comm 1236
Kimblin C, Allen WE, Parkin G (1995) J Chem Soc Chem Commun 1813
Eriksson AE, Kylsten P, Jones TA, Lilijas A (1988) Proteins, 4:283
Chen RC, Kernohan JC (1967) J Biol Chem 242:5813
Ferrer S, Borrás J, Miratvilles C, Fuertes A (1989) Inorg Chem 28:160
Koike T, Watanabe T, Kimura E, Shiro M (in press) J Am Chem Soc
Taylor PW King RW Burgen ASV (1970) Biochemistry, 9:2638
Eklund H, Jones A, Schneider G (1986) Active site in alcohol dehydrogenase. In: Bertini I, Luchinat C, Maret W Zeppezauer M (eds) Zinc enzymes. Birkhäuser, Boston p 377
Pettersson G (1986) Ionization properties of zinc-bound ligand alcohol dehydrogenase. ibid, In
Kimura E, Shionoya M, Hoshino A, Ikeda T, Yamada Y (1992) J Am Chem Soc 114:10134
Shoner SC, Humphreys KJ, Kovacs JA (1995) Inorg Chem 34:5933
Kim EE, Wyckoff HW (1991) J Mol Biol 218:449
Sigman DS, Jorgensen CT (1972) J Am Chem Soc 94:1724
Dugas H (1989) Bioorganic chemistry. Springer, Berlin Heiderberg New York, p 196
Cruickshank P, Sheehan JC (1963) J Am Chem Soc 86:2070
Vandersteen AM, Janda KD (1996) J Am Chem Soc 118:8787
Zeppezauer M (1986) The metal environment of alcohol dehydrogenase: aspects of chemical speciation and catalytic efficiency in biological catalyst. In: Bertini I, Luchinat C, Maret W Zeppezauer M (eds) Zinc enzymes. Birkhäuser, Boston, p 416
Fujioka H, Koike T, Yamada N, Kimura E (1996) Heterocycles, 42:775
Kady IO, Tan B, Ho Z, Scarborough T (1995) J Chem Soc Chem Commun 1137
Morrow JR, Aures K, Epstein D (1995) J Chem Soc Chem Commun 2431
Young MJ, Wahnon D, Hynes RC, Chin J (1995) J Chem Soc Chem Commun 9441
Kiefer LL, Ippolito JA, Fierke CA, Christianson DW (1993) J Am Chem Soc 115:12581
Krebs JK, Fierke CA (1993) J Biol Chem 268:948
Krebs JK, Ippolito JA, Christianson DW, Fierke CA (1993) J Biol Chem 268:27458
Kiefer LL, Paterno SA, Fierke CA (1995) J Am Chem Soc 117:6831
Xu X, Qin X, Kantrowitz ER (1994) Biochemistry, 33:2279
Xu X, Kantrowitz ER (1992) J Biol Chem 267:16244
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Kimura, E., Koike, T., Shionoya, M. (1997). Advances in Zinc Enzyme Models by Small, Mononuclear Zinc (II) Complexes. In: Hill, H.A.O., Sadler, P.J., Thomson, A.J. (eds) Metal Sites in Proteins and Models. Structure and Bonding, vol 89. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-62874-6_7
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