메뉴 건너뛰기




Volumn 5, Issue 10, 2010, Pages 933-942

Structural basis for adenosylcobalamin activation in adocbl-dependent ribonucleotide reductases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; COBAMAMIDE; CYSTEINE; GUANOSINE DIPHOSPHATE; HYDROGEN; PROPIONAMIDE DERIVATIVE; RIBONUCLEOTIDE REDUCTASE; RIBONUCLEOTIDE REDUCTASE 2; THIOL GROUP; THYMIDINE TRIPHOSPHATE; UNCLASSIFIED DRUG;

EID: 77958085972     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb1000845     Document Type: Article
Times cited : (36)

References (40)
  • 4
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • Licht, S., Gerfen, G. J., and Stubbe, J. (1996) Thiyl radicals in ribonucleotide reductases Science 271, 477-481
    • (1996) Science , vol.271 , pp. 477-481
    • Licht, S.1    Gerfen, G.J.2    Stubbe, J.3
  • 5
    • 0015911796 scopus 로고
    • Direct spectrophotometric observation of an intermediate formed from deoxyadenosylcobalamin in ribonucleotide reduction
    • Tamao, Y. and Blakley, R. L. (1973) Direct spectrophotometric observation of an intermediate formed from deoxyadenosylcobalamin in ribonucleotide reduction Biochemistry 12, 24-34
    • (1973) Biochemistry , vol.12 , pp. 24-34
    • Tamao, Y.1    Blakley, R.L.2
  • 6
    • 21844449665 scopus 로고    scopus 로고
    • Chemistry and enzymology of vitamin B12
    • Brown, K. L. (2005) Chemistry and enzymology of vitamin B12 Chem. Rev. 105, 2075-2149
    • (2005) Chem. Rev. , vol.105 , pp. 2075-2149
    • Brown, K.L.1
  • 7
    • 32944471990 scopus 로고    scopus 로고
    • The enzymatic activation of coenzyme B12
    • Brown, K. L. (2006) The enzymatic activation of coenzyme B12 Dalton Trans. 1123-1133
    • (2006) Dalton Trans. , pp. 1123-1133
    • Brown, K.L.1
  • 8
    • 0037560995 scopus 로고    scopus 로고
    • Radical catalysis in coenzyme B12-dependent isomerization (eliminating) reactions
    • Toraya, T. (2003) Radical catalysis in coenzyme B12-dependent isomerization (eliminating) reactions Chem. Rev. 103, 2095-2127
    • (2003) Chem. Rev. , vol.103 , pp. 2095-2127
    • Toraya, T.1
  • 9
    • 0041766196 scopus 로고    scopus 로고
    • The many faces of vitamin B12: Catalysis by cobalamin-dependent enzymes
    • Banerjee, R. and Ragsdale, S. W. (2003) The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes Annu. Rev. Biochem. 72, 209-247
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 209-247
    • Banerjee, R.1    Ragsdale, S.W.2
  • 10
    • 21344463602 scopus 로고    scopus 로고
    • How the Co-C bond is cleaved in coenzyme B12 enzymes: A theoretical study
    • Jensen, K. P. and Ryde, U. (2005) How the Co-C bond is cleaved in coenzyme B12 enzymes: a theoretical study J. Am. Chem. Soc. 127, 9117-9128
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9117-9128
    • Jensen, K.P.1    Ryde, U.2
  • 11
    • 34547457947 scopus 로고    scopus 로고
    • A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes
    • Sharma, P. K., Chu, Z. T., Olsson, M. H., and Warshel, A. (2007) A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes Proc. Natl. Acad. Sci. U.S.A. 104, 9661-9666
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 9661-9666
    • Sharma, P.K.1    Chu, Z.T.2    Olsson, M.H.3    Warshel, A.4
  • 12
    • 0037159207 scopus 로고    scopus 로고
    • Substrate-induced conformational change of a coenzyme B12-dependent enzyme: Crystal structure of the substrate-free form of diol dehydratase
    • Shibata, N., Masuda, J., Morimoto, Y., Yasuoka, N., and Toraya, T. (2002) Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase Biochemistry 41, 12607-12617
    • (2002) Biochemistry , vol.41 , pp. 12607-12617
    • Shibata, N.1    Masuda, J.2    Morimoto, Y.3    Yasuoka, N.4    Toraya, T.5
  • 13
    • 0034661847 scopus 로고    scopus 로고
    • How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex
    • Masuda, J., Shibata, N., Morimoto, Y., Toraya, T., and Yasuoka, N. (2000) How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex Structure 8, 775-788
    • (2000) Structure , vol.8 , pp. 775-788
    • Masuda, J.1    Shibata, N.2    Morimoto, Y.3    Toraya, T.4    Yasuoka, N.5
  • 15
    • 0035903592 scopus 로고    scopus 로고
    • Radical shuttling in a protein: Ribose pseudorotation controls alkyl-radical transfer in the coenzyme B(12) dependent enzyme glutamate mutase
    • Gruber, K., Reitzer, R., and Kratky, C. (2001) Radical shuttling in a protein: Ribose pseudorotation controls alkyl-radical transfer in the coenzyme B(12) dependent enzyme glutamate mutase Angew. Chem., Int. Ed. 40, 3377-3380
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 3377-3380
    • Gruber, K.1    Reitzer, R.2    Kratky, C.3
  • 16
    • 0033604871 scopus 로고    scopus 로고
    • Studies on the catalysis of carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: Evidence for concerted carbon-cobalt bond homolysis and thiyl radical formation
    • Licht, S. S., Booker, S., and Stubbe, J. (1999) Studies on the catalysis of carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: evidence for concerted carbon-cobalt bond homolysis and thiyl radical formation Biochemistry 38, 1221-1233
    • (1999) Biochemistry , vol.38 , pp. 1221-1233
    • Licht, S.S.1    Booker, S.2    Stubbe, J.3
  • 17
    • 0033604854 scopus 로고    scopus 로고
    • Thermodynamic and kinetic studies on carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: The importance of entropy in catalysis
    • Licht, S. S., Lawrence, C. C., and Stubbe, J. (1999) Thermodynamic and kinetic studies on carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: the importance of entropy in catalysis Biochemistry 38, 1234-1242
    • (1999) Biochemistry , vol.38 , pp. 1234-1242
    • Licht, S.S.1    Lawrence, C.C.2    Stubbe, J.3
  • 18
    • 0032560980 scopus 로고    scopus 로고
    • Activation parameters for the carbon-cobalt bond homolysis of coenzyme B-12 induced by the B-12-dependent ribonucleotide reductase from Lactobacillus leichmannii
    • Brown, K. L. and Li, J. (1998) Activation parameters for the carbon-cobalt bond homolysis of coenzyme B-12 induced by the B-12-dependent ribonucleotide reductase from Lactobacillus leichmannii J. Am. Chem. Soc. 120, 9466-9474
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9466-9474
    • Brown, K.L.1    Li, J.2
  • 19
    • 0037461322 scopus 로고    scopus 로고
    • Epimerization at carbon-5' of (5' R)-[5'-2 H ]adenosylcobalamin by ribonucleoside triphosphate reductase: Cysteine 408-independent cleavage of the Co-C5' bond
    • Chen, D., Abend, A., Stubbe, J., and Frey, P. A. (2003) Epimerization at carbon-5' of (5' R)-[5'-2 H ]adenosylcobalamin by ribonucleoside triphosphate reductase: cysteine 408-independent cleavage of the Co-C5' bond Biochemistry 42, 4578-4584
    • (2003) Biochemistry , vol.42 , pp. 4578-4584
    • Chen, D.1    Abend, A.2    Stubbe, J.3    Frey, P.A.4
  • 20
    • 0036219377 scopus 로고    scopus 로고
    • The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer
    • Sintchak, M. D., Arjara, G., Kellogg, B. A., Stubbe, J., and Drennan, C. L. (2002) The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer Nat. Struct. Biol. 9, 293-300
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 293-300
    • Sintchak, M.D.1    Arjara, G.2    Kellogg, B.A.3    Stubbe, J.4    Drennan, C.L.5
  • 21
    • 0029841914 scopus 로고    scopus 로고
    • Electron paramagnetic resonance observations of a kinetically competent intermediate formed in ribonucleotide reduction: Evidence for a thiyl radical-cob(II)alamin interaction
    • Gerfen, G. J., Licht, S., Willems, J. P., Hoffmann, B. M., and Stubbe, J. (1996) Electron paramagnetic resonance observations of a kinetically competent intermediate formed in ribonucleotide reduction: evidence for a thiyl radical-cob(II)alamin interaction J. Am. Chem. Soc. 118, 8192-8197
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8192-8197
    • Gerfen, G.J.1    Licht, S.2    Willems, J.P.3    Hoffmann, B.M.4    Stubbe, J.5
  • 22
    • 0031471116 scopus 로고    scopus 로고
    • B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli
    • Jordan, A., Torrents, E., Jeanthon, C., Eliasson, R., Hellman, U., Wernstedt, C., Barbeé, J., and Reichard, P. (1997) B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 94, 13487-13492
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13487-13492
    • Jordan, A.1    Torrents, E.2    Jeanthon, C.3    Eliasson, R.4    Hellman, U.5    Wernstedt, C.6    Barbeé, J.7    Reichard, P.8
  • 23
    • 0033548274 scopus 로고    scopus 로고
    • 12-dependent (Class II) ribonucleotide reductases. Implications for the evolution of ribonucleotide reduction
    • 12-dependent (Class II) ribonucleotide reductases. Implications for the evolution of ribonucleotide reduction J. Biol. Chem. 274, 7182-7189
    • (1999) J. Biol. Chem. , vol.274 , pp. 7182-7189
    • Eliasson, R.1    Pontis, E.2    Jordan, A.3    Reichard, P.4
  • 24
    • 73149106387 scopus 로고    scopus 로고
    • RNRdb, a curated database of the universal enzyme family ribonucleotide reductase, reveals a high level of misannotation in sequences deposited to Genbank
    • Lundin, D., Torrents, E., Poole, A. M., and Sjoberg, B. M. (2009) RNRdb, a curated database of the universal enzyme family ribonucleotide reductase, reveals a high level of misannotation in sequences deposited to Genbank BMC Genomics 10, 589
    • (2009) BMC Genomics , vol.10 , pp. 589
    • Lundin, D.1    Torrents, E.2    Poole, A.M.3    Sjoberg, B.M.4
  • 25
    • 7544227865 scopus 로고    scopus 로고
    • Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase
    • Larsson, K. M., Jordan, A., Eliasson, R., Reichard, P., Logan, D. T., and Nordlund, P. (2004) Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase Nat. Struct. Mol. Biol. 11, 1142-1149
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1142-1149
    • Larsson, K.M.1    Jordan, A.2    Eliasson, R.3    Reichard, P.4    Logan, D.T.5    Nordlund, P.6
  • 26
    • 0035813257 scopus 로고    scopus 로고
    • Enzymatic activity of coenzyme B(12) derivatives with altered axial nucleotides: Probing the mechanochemical triggering hypothesis in ribonucleotide reductase
    • Brown, K. L., Zou, X., Li, J., and Chen, G. (2001) Enzymatic activity of coenzyme B(12) derivatives with altered axial nucleotides: probing the mechanochemical triggering hypothesis in ribonucleotide reductase Inorg. Chem. 40, 5942-5947
    • (2001) Inorg. Chem. , vol.40 , pp. 5942-5947
    • Brown, K.L.1    Zou, X.2    Li, J.3    Chen, G.4
  • 27
    • 17344380696 scopus 로고    scopus 로고
    • Stabilization of the adenosyl radical in coenzyme B-12î - ̧a theoretical study
    • Dólker, N., Maseras, F., and Siegbahn, P. E. M. (2004) Stabilization of the adenosyl radical in coenzyme B-12î - ̧a theoretical study Chem. Phys. Lett. 386, 174-178
    • (2004) Chem. Phys. Lett. , vol.386 , pp. 174-178
    • Dólker, N.1    Maseras, F.2    Siegbahn, P.E.M.3
  • 28
    • 0033603831 scopus 로고    scopus 로고
    • Class II ribonucleotide reductases catalyze carbon-cobalt bond reformation on every turnover
    • DOI 10.1021/ja9913840
    • Licht, S. S., Lawrence, C. C., and Stubbe, J. (1999) Class II ribonucleotide reductases catalyze carbon-cobalt bond reformation on every turnover J. Am. Chem. Soc. 121, 7463-7468 (Pubitemid 29413706)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.33 , pp. 7463-7468
    • Licht, S.S.1    Lawrence, C.C.2    Stubbe, J.3
  • 29
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • Uhlin, U. and Eklund, H. (1994) Structure of ribonucleotide reductase protein R1 Nature 370, 533-539
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 30
    • 0033525599 scopus 로고    scopus 로고
    • A glycyl radical site in the crystal structure of a class III ribonucleotide reductase
    • Logan, D. T., Andersson, J., Sjóberg, B.-M., and Nordlund, P. (1999) A glycyl radical site in the crystal structure of a class III ribonucleotide reductase Science 283, 1499-1504
    • (1999) Science , vol.283 , pp. 1499-1504
    • Logan, D.T.1    Andersson, J.2    Sjóberg, B.-M.3    Nordlund, P.4
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • in (, Eds.), pp - 326, Academic Press, New York.
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, in Methods in Enzymology (Carter, C. W., Jr. and Sweet, R. M., Eds.), pp 307 - 326, Academic Press, New York.
    • (1997) Methods in Enzymology , pp. 307
    • Otwinowski, Z.1    Minor, W.2    Carter Jr., C.W.3    Sweet, R.M.4
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, no. 4 ((), - 763.
    • Collaborative Computational Project, no. 4 ((1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760 - 763.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760
  • 36
    • 1242317113 scopus 로고    scopus 로고
    • Accurate redetermination of the X-ray structure and electronic bonding in adenosylcobalamin
    • Ouyang, L., Rulis, P., Ching, W. Y., Nardin, G., and Randaccio, L. (2004) Accurate redetermination of the X-ray structure and electronic bonding in adenosylcobalamin Inorg. Chem. 43, 1235-1241
    • (2004) Inorg. Chem. , vol.43 , pp. 1235-1241
    • Ouyang, L.1    Rulis, P.2    Ching, W.Y.3    Nardin, G.4    Randaccio, L.5
  • 37
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard (1991) Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A47 (Pt 2) 110-119
    • (1991) Acta Crystallogr. , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 39
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E. and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr., Sect. D: Biol. Crystallogr. 60, 2256-2268
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.