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Volumn 1804, Issue 2, 2010, Pages 422-426

Proton transfer in catalysis and the role of proton shuttles in carbonic anhydrase

Author keywords

Bicarbonate; Carbon dioxide; Carbonic anhydrase; Hydration; Proton transfer

Indexed keywords

CARBON DIOXIDE; CARBONATE DEHYDRATASE; IMIDAZOLE; PROTON;

EID: 74449085230     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.08.003     Document Type: Review
Times cited : (79)

References (36)
  • 1
    • 0016722749 scopus 로고
    • Catalytic mechanism of carbonic-anhydrase - hydrogen-isotope effects on kinetic-parameters of human C isoenzyme
    • Steiner H., Jonsson B.H., and Lindskog S. Catalytic mechanism of carbonic-anhydrase - hydrogen-isotope effects on kinetic-parameters of human C isoenzyme. Eur. J. Biochem. 59 (1975) 253-259
    • (1975) Eur. J. Biochem. , vol.59 , pp. 253-259
    • Steiner, H.1    Jonsson, B.H.2    Lindskog, S.3
  • 2
    • 0024421430 scopus 로고
    • Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant
    • Tu C.K., Silverman D.N., Forsman C., Jonsson B.H., and Lindskog S. Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant. Biochemistry 28 (1989) 7913-7918
    • (1989) Biochemistry , vol.28 , pp. 7913-7918
    • Tu, C.K.1    Silverman, D.N.2    Forsman, C.3    Jonsson, B.H.4    Lindskog, S.5
  • 3
    • 33845278732 scopus 로고
    • The catalytic mechanism of carbonic-anhydrase - implications of a rate-limiting protolysis of water
    • Silverman D.N., and Lindskog S. The catalytic mechanism of carbonic-anhydrase - implications of a rate-limiting protolysis of water. Acc. Chem. Res. 21 (1988) 30-36
    • (1988) Acc. Chem. Res. , vol.21 , pp. 30-36
    • Silverman, D.N.1    Lindskog, S.2
  • 8
    • 0009593678 scopus 로고
    • Unexpected pH-dependent conformation of His-64, the proton shuttle of carbonic anhydrase-II
    • Nair S.K., and Christianson D.W. Unexpected pH-dependent conformation of His-64, the proton shuttle of carbonic anhydrase-II. J. Am. Chem. Soc. 113 (1991) 9455-9458
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9455-9458
    • Nair, S.K.1    Christianson, D.W.2
  • 11
    • 0034622565 scopus 로고    scopus 로고
    • A structure-function study of a proton transport pathway in the gamma-class carbonic anhydrase from Methanosarcina thermophila
    • Tripp B.C., and Ferry J.G. A structure-function study of a proton transport pathway in the gamma-class carbonic anhydrase from Methanosarcina thermophila. Biochemistry 39 (2000) 9232-9240
    • (2000) Biochemistry , vol.39 , pp. 9232-9240
    • Tripp, B.C.1    Ferry, J.G.2
  • 12
    • 0034622579 scopus 로고    scopus 로고
    • A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila
    • Iverson T.M., Alber B.E., Kisker C., Ferry J.G., and Rees D.C. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry 39 (2000) 9222-9231
    • (2000) Biochemistry , vol.39 , pp. 9222-9231
    • Iverson, T.M.1    Alber, B.E.2    Kisker, C.3    Ferry, J.G.4    Rees, D.C.5
  • 14
    • 0037176904 scopus 로고    scopus 로고
    • Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle
    • Jude K.M., Wright S.K., Tu C., Silverman D.N., Viola R.E., and Christianson D.W. Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle. Biochemistry 41 (2002) 2485-2491
    • (2002) Biochemistry , vol.41 , pp. 2485-2491
    • Jude, K.M.1    Wright, S.K.2    Tu, C.3    Silverman, D.N.4    Viola, R.E.5    Christianson, D.W.6
  • 15
    • 34548724094 scopus 로고    scopus 로고
    • Solvent-mediated proton transfer in catalysis by carbonic anhydrase
    • Silverman D.N., and McKenna R. Solvent-mediated proton transfer in catalysis by carbonic anhydrase. Acc. Chem. Res. 40 (2007) 669-675
    • (2007) Acc. Chem. Res. , vol.40 , pp. 669-675
    • Silverman, D.N.1    McKenna, R.2
  • 16
    • 33947367836 scopus 로고    scopus 로고
    • Preferred orientations of His64 in human carbonic anhydrase II
    • Maupin C.M., and Voth G.A. Preferred orientations of His64 in human carbonic anhydrase II. Biochemistry 46 (2007) 2938-2947
    • (2007) Biochemistry , vol.46 , pp. 2938-2947
    • Maupin, C.M.1    Voth, G.A.2
  • 17
    • 67650513577 scopus 로고    scopus 로고
    • Elucidation of the proton transport mechanism in human carbonic anhydrase II
    • Maupin C.M., McKenna R., Silverman D.N., and Voth G.A. Elucidation of the proton transport mechanism in human carbonic anhydrase II. J. Am. Chem. Soc. 131 (2009) 7598-7608
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7598-7608
    • Maupin, C.M.1    McKenna, R.2    Silverman, D.N.3    Voth, G.A.4
  • 18
    • 0027427176 scopus 로고
    • Proton-transfer in the catalytic mechanism of carbonic-anhydrase. 2. Effects of placing histidine-residues at various positions in the active-site of human isoenzyme-II
    • Liang Z.W., Jonsson B.H., and Lindskog S. Proton-transfer in the catalytic mechanism of carbonic-anhydrase. 2. Effects of placing histidine-residues at various positions in the active-site of human isoenzyme-II. Biochim. Biophys. Acta 1203 (1993) 142-146
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 142-146
    • Liang, Z.W.1    Jonsson, B.H.2    Lindskog, S.3
  • 19
    • 39749169756 scopus 로고    scopus 로고
    • Proton transfer in carbonic anhydrase is controlled by electrostatics rather than the orientation of the acceptor
    • Riccardi D., Konig P., Guo H., and Cui Q. Proton transfer in carbonic anhydrase is controlled by electrostatics rather than the orientation of the acceptor. Biochemistry 47 (2008) 2369-2378
    • (2008) Biochemistry , vol.47 , pp. 2369-2378
    • Riccardi, D.1    Konig, P.2    Guo, H.3    Cui, Q.4
  • 20
    • 0025946277 scopus 로고
    • Conformational mobility of His-64 in the Thr200Ser mutant of human carbonic anhydrase-II
    • Krebs J.F., Fierke C.A., Alexander R.S., and Christianson D.W. Conformational mobility of His-64 in the Thr200Ser mutant of human carbonic anhydrase-II. Biochemistry 30 (1991) 9153-9160
    • (1991) Biochemistry , vol.30 , pp. 9153-9160
    • Krebs, J.F.1    Fierke, C.A.2    Alexander, R.S.3    Christianson, D.W.4
  • 21
    • 0020346412 scopus 로고
    • Carbonic anhydrase: oxygen-18 exchange catalyzed by an enzyme with rate-contributing proton-transfer steps
    • Silverman D.N. Carbonic anhydrase: oxygen-18 exchange catalyzed by an enzyme with rate-contributing proton-transfer steps. Methods Enzymol. 87 (1982) 732-752
    • (1982) Methods Enzymol. , vol.87 , pp. 732-752
    • Silverman, D.N.1
  • 22
    • 33947684326 scopus 로고    scopus 로고
    • Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitution in the active site of human carbonic anhydrase II
    • Fisher S.Z., Tu C.K., Bhatt D., Govindasamy L., Agbandje-McKenna M., McKenna R., and Silverman D.N. Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitution in the active site of human carbonic anhydrase II. Biochemistry 42 (2007) 3803-3813
    • (2007) Biochemistry , vol.42 , pp. 3803-3813
    • Fisher, S.Z.1    Tu, C.K.2    Bhatt, D.3    Govindasamy, L.4    Agbandje-McKenna, M.5    McKenna, R.6    Silverman, D.N.7
  • 23
    • 56249123954 scopus 로고    scopus 로고
    • Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II
    • Zheng J.Y., Avvaru B.S., Tu C., McKenna R., and Silverman D.N. Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II. Biochemistry 47 (2008) 12028-12036
    • (2008) Biochemistry , vol.47 , pp. 12028-12036
    • Zheng, J.Y.1    Avvaru, B.S.2    Tu, C.3    McKenna, R.4    Silverman, D.N.5
  • 25
    • 0027438252 scopus 로고
    • Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase III
    • Silverman D.N., Tu C., Chen X., Tanhauser S.M., Kresge A.J., and Laipis P.J. Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase III. Biochemistry 32 (1993) 10757-10762
    • (1993) Biochemistry , vol.32 , pp. 10757-10762
    • Silverman, D.N.1    Tu, C.2    Chen, X.3    Tanhauser, S.M.4    Kresge, A.J.5    Laipis, P.J.6
  • 26
    • 0032823542 scopus 로고    scopus 로고
    • Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions
    • Kresge A.J., and Silverman D.N. Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions. Enzym. Kinet. Mech. Pt E 308 (1999) 276-297
    • (1999) Enzym. Kinet. Mech. , vol.PART E 308 , pp. 276-297
    • Kresge, A.J.1    Silverman, D.N.2
  • 27
    • 12344266417 scopus 로고    scopus 로고
    • Studies of proton translocations in biological systems: simulating proton transport in carbonic anhydrase by EVB-based models
    • Braun-Sand S., Strajbl M., and Warshel A. Studies of proton translocations in biological systems: simulating proton transport in carbonic anhydrase by EVB-based models. Biophys. J. 87 (2004) 2221-2239
    • (2004) Biophys. J. , vol.87 , pp. 2221-2239
    • Braun-Sand, S.1    Strajbl, M.2    Warshel, A.3
  • 28
    • 0037473097 scopus 로고    scopus 로고
    • Is a "proton wire" concerted or stepwise? A model study of proton transfer in carbonic anhydrase
    • Cui Q., and Karplus M. Is a "proton wire" concerted or stepwise? A model study of proton transfer in carbonic anhydrase. J. Phys. Chem. B 107 (2003) 1071-1078
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1071-1078
    • Cui, Q.1    Karplus, M.2
  • 29
    • 0041843738 scopus 로고    scopus 로고
    • A computer simulation study of the hydrated proton in a synthetic proton channel
    • Wu Y., and Voth G.A. A computer simulation study of the hydrated proton in a synthetic proton channel. Biophys. J. 85 (2003) 864-875
    • (2003) Biophys. J. , vol.85 , pp. 864-875
    • Wu, Y.1    Voth, G.A.2
  • 30
    • 0035070279 scopus 로고    scopus 로고
    • The formation and dynamics of proton wires in channel environments
    • Brewer M.L., Schmitt U.W., and Voth G.A. The formation and dynamics of proton wires in channel environments. Biophys. J. 80 (2001) 1691-1702
    • (2001) Biophys. J. , vol.80 , pp. 1691-1702
    • Brewer, M.L.1    Schmitt, U.W.2    Voth, G.A.3
  • 31
    • 61849141323 scopus 로고    scopus 로고
    • A theory-experiment conundrum for proton transfer
    • Peters K.S. A theory-experiment conundrum for proton transfer. Acc. Chem. Res. 42 (2009) 89-96
    • (2009) Acc. Chem. Res. , vol.42 , pp. 89-96
    • Peters, K.S.1
  • 33
    • 16244403026 scopus 로고    scopus 로고
    • Proton transfer from exogenous donors in catalysis by human carbonic anhydrase II
    • Elder I., Tu C.K., Ming L.J., McKenna R., and Silverman D.N. Proton transfer from exogenous donors in catalysis by human carbonic anhydrase II. Arch. Biochem. Biophys. 437 (2005) 106-114
    • (2005) Arch. Biochem. Biophys. , vol.437 , pp. 106-114
    • Elder, I.1    Tu, C.K.2    Ming, L.J.3    McKenna, R.4    Silverman, D.N.5
  • 35
    • 13444269025 scopus 로고    scopus 로고
    • Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II
    • Fisher Z., Prada J.A.H., Tu C., Duda D., Yoshioka C., An H.Q., Govindasamy L., Silverman D.N., and McKenna R. Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II. Biochemistry 44 (2005) 1097-1105
    • (2005) Biochemistry , vol.44 , pp. 1097-1105
    • Fisher, Z.1    Prada, J.A.H.2    Tu, C.3    Duda, D.4    Yoshioka, C.5    An, H.Q.6    Govindasamy, L.7    Silverman, D.N.8    McKenna, R.9
  • 36
    • 33846417994 scopus 로고    scopus 로고
    • Location of binding sites in small molecule rescue of human carbonic anhydrase II
    • Bhatt D., Fisher S.Z., Tu C., McKenna R., and Silverman D.N. Location of binding sites in small molecule rescue of human carbonic anhydrase II. Biophys. J. 92 (2007) 562-570
    • (2007) Biophys. J. , vol.92 , pp. 562-570
    • Bhatt, D.1    Fisher, S.Z.2    Tu, C.3    McKenna, R.4    Silverman, D.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.