메뉴 건너뛰기




Volumn 36, Issue 7, 2003, Pages 522-529

ENDOR of metalloenzymes

Author keywords

[No Author keywords available]

Indexed keywords

ALLYLBENZENE INACTIVATED CHLOROPEROXIDASE; CHLORIDE PEROXIDASE; CYTOCHROME C PEROXIDASE; ENZYME; IRON DERIVATIVE; METALLOENZYME; OXYGEN; RIBONUCLEOTIDE REDUCTASE; S ADENOSYLMETHIONINE; SULFUR DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0038506974     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar0202565     Document Type: Article
Times cited : (79)

References (40)
  • 1
    • 0000907326 scopus 로고
    • Electron nuclear double resonance (ENDOR) of metalloenzymes
    • Hoffman, B. M. Electron nuclear double resonance (ENDOR) of metalloenzymes. Acc. Chem. Res. 1991, 24, 164-170.
    • (1991) Acc. Chem. Res. , vol.24 , pp. 164-170
    • Hoffman, B.M.1
  • 4
    • 0002826498 scopus 로고    scopus 로고
    • Q-Band Pulsed Electron Spin-Echo Spectrometer and Its Application to ENDOR and ESEEM
    • Davoust, C. E.; Doan, P. E.; Hoffman, B. M. Q-Band Pulsed Electron Spin-Echo Spectrometer and Its Application to ENDOR and ESEEM. J. Magn. Reson. 1996, 119, 38-44.
    • (1996) J. Magn. Reson. , vol.119 , pp. 38-44
    • Davoust, C.E.1    Doan, P.E.2    Hoffman, B.M.3
  • 7
    • 0028963868 scopus 로고
    • Protein Structure and Mechanism Studied by Electron Nuclear Double Resonance Spectroscopy
    • DeRose, V. J.; Hoffman, B. M. Protein Structure and Mechanism Studied by Electron Nuclear Double Resonance Spectroscopy. Methods Enzymol. 1995, 246, 554-589.
    • (1995) Methods Enzymol. , vol.246 , pp. 554-589
    • DeRose, V.J.1    Hoffman, B.M.2
  • 8
    • 33748244205 scopus 로고
    • Pulsed Electron Spin Resonance Spectroscopy: Basic Principles, Techniques, and Examples of Applications
    • Schweiger, A. Pulsed Electron Spin Resonance Spectroscopy: Basic Principles, Techniques, and Examples of Applications. Ang. Chem., Int. Ed. Engl. 1991, 30, 265-292.
    • (1991) Ang. Chem., Int. Ed. Engl. , vol.30 , pp. 265-292
    • Schweiger, A.1
  • 9
    • 0005943092 scopus 로고
    • Spin and magnetic moment of p22 by the electron nuclear double-resonance technique
    • Feher, G.; Fuller, C. S.; Gere, E. A. Spin and magnetic moment of p22 by the electron nuclear double-resonance technique. Phys. Rev. 1957, 107, 1462-4.
    • (1957) Phys. Rev. , vol.107 , pp. 1462-1464
    • Feher, G.1    Fuller, C.S.2    Gere, E.A.3
  • 10
    • 0031547577 scopus 로고    scopus 로고
    • Making hyperfine selection in Mims ENDOR independent of deadtime
    • Doan, P. E.; Hoffman, B. M. Making hyperfine selection in Mims ENDOR independent of deadtime. Chem. Phys. Lett. 1997, 269, 208-214.
    • (1997) Chem. Phys. Lett. , vol.269 , pp. 208-214
    • Doan, P.E.1    Hoffman, B.M.2
  • 11
    • 0017083127 scopus 로고
    • Assignment of a ligand in stellacyanin by a pulsed electron paramagnetic resonance method
    • Mims, W. B.; Peisach, J. Assignment of a ligand in stellacyanin by a pulsed electron paramagnetic resonance method. Biochemistry 1976, 15, 3863-3869.
    • (1976) Biochemistry , vol.15 , pp. 3863-3869
    • Mims, W.B.1    Peisach, J.2
  • 14
    • 0029740493 scopus 로고    scopus 로고
    • Reconsideration of X, the Diiron Intermediate Formed during Cofactor Assembly in E. coli Ribonucleotide Reductase
    • Sturgeon, B. E.; Burdi, D.; Chen, S.; Huynh, B. H.; Edmondson, D. E.; Stubbe, J.; Hoffman, B. M. Reconsideration of X, the Diiron Intermediate Formed during Cofactor Assembly in E. coli Ribonucleotide Reductase. J. Am. Chem. Soc. 1996, 118, 7551-7557.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7551-7557
    • Sturgeon, B.E.1    Burdi, D.2    Chen, S.3    Huynh, B.H.4    Edmondson, D.E.5    Stubbe, J.6    Hoffman, B.M.7
  • 18
    • 0000426525 scopus 로고
    • The determination of hydrogen coordinates in lanthanum nicotinate dihydrate crystals by Nd-{+3}-proton double resonance
    • Hutchison, C. A., Jr.; McKay, D. B. The determination of hydrogen coordinates in lanthanum nicotinate dihydrate crystals by Nd-{+3}-proton double resonance. J. Chem. Phys. 1977, 66, 3311-3330.
    • (1977) J. Chem. Phys. , vol.66 , pp. 3311-3330
    • Hutchison C.A., Jr.1    McKay, D.B.2
  • 19
    • 0007847119 scopus 로고
    • Electron Spin-Echo Envelope Modulation in Randomly Oriented Doublet and Triplet Systems
    • de Groot, A.; Evelo, R.; Hoff, A. Electron Spin-Echo Envelope Modulation in Randomly Oriented Doublet and Triplet Systems. J. J. Magn. Reson. 1986, 66, 331-343.
    • (1986) J. J. Magn. Reson. , vol.66 , pp. 331-343
    • De Groot, A.1    Evelo, R.2    Hoff, A.3
  • 20
    • 0035954401 scopus 로고    scopus 로고
    • Fast Deuterium Access to the Buried Magnesium/Manganese Site in Cytochrome c Oxidase
    • Florens, L.; Schmidt, B.; McCracken, J., Ferguson-Miller, S. Fast Deuterium Access to the Buried Magnesium/Manganese Site in Cytochrome c Oxidase. Biochemistry 2001, 40, 7491-7497.
    • (2001) Biochemistry , vol.40 , pp. 7491-7497
    • Florens, L.1    Schmidt, B.2    McCracken, J.3    Ferguson-Miller, S.4
  • 21
    • 0029637916 scopus 로고
    • Compound ES of Cytochrome c Peroxidase Contains a Trp π-Cation Radical: Characterization by CW and Pulsed Q-Band ENDOR
    • Huyett, J. E.; Doan, P. E.; Gurbiel, R.; Houseman, A. L. P.; Sivaraja, M.; Goodin, D. B.; Hoffman, B. M. Compound ES of Cytochrome c Peroxidase Contains a Trp π-Cation Radical: Characterization by CW and Pulsed Q-Band ENDOR. J. Am. Chem. Soc. 1995, 117, 9033-9041.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9033-9041
    • Huyett, J.E.1    Doan, P.E.2    Gurbiel, R.3    Houseman, A.L.P.4    Sivaraja, M.5    Goodin, D.B.6    Hoffman, B.M.7
  • 26
    • 0027951575 scopus 로고
    • Mechanism of Assembly of the Tyrosyl Radical-Diiron-(III) Cofactor of E. Coli Ribonucleotide Reductase. 1. Mössbauer Characterization of the Diferric Radical Precursor
    • Ravi, N.; Bollinger, J. M., Jr.; Huynh, B. H.; Edmondson, D. E.; Stubbe, J. Mechanism of Assembly of the Tyrosyl Radical-Diiron-(III) Cofactor of E. Coli Ribonucleotide Reductase. 1. Mössbauer Characterization of the Diferric Radical Precursor. J. Am. Chem. Soc. 1994, 116, 8007-8014.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8007-8014
    • Ravi, N.1    Bollinger J.M., Jr.2    Huynh, B.H.3    Edmondson, D.E.4    Stubbe, J.5
  • 27
    • 0030908542 scopus 로고    scopus 로고
    • Structure of the Modified Heme in Allylbenzene-Inactivated Chloroperoxidase Determined by Q-Band CW and Pulsed ENDOR
    • Lee, H.-I.; Dexter, A. F.; Fann, Y.-C.; Lakner, F. J.; Hager, L. P.; Hoffman, B. M. Structure of the Modified Heme in Allylbenzene-Inactivated Chloroperoxidase Determined by Q-Band CW and Pulsed ENDOR. J. Am. Chem. Soc. 1997, 119, 4059-4069.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4059-4069
    • Lee, H.-I.1    Dexter, A.F.2    Fann, Y.-C.3    Lakner, F.J.4    Hager, L.P.5    Hoffman, B.M.6
  • 28
    • 0029103571 scopus 로고
    • Transient Heme N-Alkylation of Chloroperoxidase by Terminal Alkenes and Alkynes
    • Dexter, A. F.; Hager, L. P. Transient Heme N-Alkylation of Chloroperoxidase by Terminal Alkenes and Alkynes. J. Am. Chem. Soc. 1995, 117, 817-818.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 817-818
    • Dexter, A.F.1    Hager, L.P.2
  • 30
    • 0037174377 scopus 로고    scopus 로고
    • An Anchoring Role for FeS Clusters: Chelation of the Amino Acid Moiety of S-Adenosylmethionine to the Unique Iron Site of the [4Fe-4S] Cluster of Pyruvate Formate-Lyase Activating Enzyme
    • Walsby, C. J.; Ortillo, D.; Broderick, W. E.; Broderick, J. B.; Hoffman, B. M. An Anchoring Role for FeS Clusters: Chelation of the Amino Acid Moiety of S-Adenosylmethionine to the Unique Iron Site of the [4Fe-4S] Cluster of Pyruvate Formate-Lyase Activating Enzyme. J. Am. Chem. Soc. 2002, 124, 11270-11271.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11270-11271
    • Walsby, C.J.1    Ortillo, D.2    Broderick, W.E.3    Broderick, J.B.4    Hoffman, B.M.5
  • 31
    • 0034841061 scopus 로고    scopus 로고
    • Adenosylmethionine-dependent iron-sulfur enzymes: Versatile clusters in a radical new role
    • Cheek, J.; Broderick, J. B. Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role. JBIC 2001, 6, 209-226.
    • (2001) JBIC , vol.6 , pp. 209-226
    • Cheek, J.1    Broderick, J.B.2
  • 32
    • 0034912671 scopus 로고    scopus 로고
    • Radical mechanisms of enzymatic catalysis
    • Frey, P. A. Radical mechanisms of enzymatic catalysis. Annu. Rev. Biochem. 2001, 70, 121-148.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 121-148
    • Frey, P.A.1
  • 33
    • 0035925164 scopus 로고    scopus 로고
    • Hydroxylation of Camphor by Reduced oxy-Cytochrome P450cam: Mechanistic Implications of EPR and ENDOR of Catalytic Intermediates in Native and Mutant Enzymes
    • Davydov, R.; Makris, T. M.; Kofman, V.; Werst, D. W.; Sligar, S. G.; Hoffman, B. M. Hydroxylation of Camphor by Reduced oxy-Cytochrome P450cam: Mechanistic Implications of EPR and ENDOR of Catalytic Intermediates in Native and Mutant Enzymes. J. Am. Chem. Soc. 2001, 123, 1403-1415.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1403-1415
    • Davydov, R.1    Makris, T.M.2    Kofman, V.3    Werst, D.W.4    Sligar, S.G.5    Hoffman, B.M.6
  • 34
    • 0037181030 scopus 로고    scopus 로고
    • Catalytic Mechanism of Heme Oxygenase through EPR and ENDOR of Cryoreduced Oxy-Heme Oxygenase and its Asp140 Mutants
    • Davydov, R.; Kofman, V.; Fujii, H.; Yoshida, T.; Ikeda-Saito, M.; Hoffman, B. Catalytic Mechanism of Heme Oxygenase through EPR and ENDOR of Cryoreduced Oxy-Heme Oxygenase and its Asp140 Mutants. J. Am. Chem. Soc. 2002, 124, 1798-1808.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1798-1808
    • Davydov, R.1    Kofman, V.2    Fujii, H.3    Yoshida, T.4    Ikeda-Saito, M.5    Hoffman, B.6
  • 35
    • 0037143567 scopus 로고    scopus 로고
    • EPR ENDOR Characterization of Intermediates in the Cryoreduced Oxy-Nitric Oxide Synthase Heme Domain with Bound L-Arginine or NG-Hydroxyarginine
    • Davydov, R.; Ledbetter-Rogers, A.; Martasek, P.; Larukhin, M.; Sono, M.; Dawson, J. H.; Siler Masters, B. S.; Hoffman, B. M. EPR and ENDOR Characterization of Intermediates in the Cryoreduced Oxy-Nitric Oxide Synthase Heme Domain with Bound L-Arginine or NG-Hydroxyarginine. Biochemistry 2002, 41, 10375-10381.
    • (2002) Biochemistry , vol.41 , pp. 10375-10381
    • Davydov, R.1    Ledbetter-Rogers, A.2    Martasek, P.3    Larukhin, M.4    Sono, M.5    Dawson, J.H.6    Siler, M.B.S.7    Hoffman, B.M.8
  • 37
    • 0034728622 scopus 로고    scopus 로고
    • Cytochrome P450-Catalyzed Hydroxylation of Mechanistic Probes that Distinguish between Radicals and Cations. Evidence for Cationic but Not for Radical Intermediates
    • Newcomb, M.; Shen, R.; Choi, S.-Y.; Toy, P. H.; Hollenberg, P. F.; Vaz, A. D. N.; Coon, M. J. Cytochrome P450-Catalyzed Hydroxylation of Mechanistic Probes that Distinguish between Radicals and Cations. Evidence for Cationic but Not for Radical Intermediates. J. Am. Chem. Soc. 2000, 122, 2677-2686.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2677-2686
    • Newcomb, M.1    Shen, R.2    Choi, S.-Y.3    Toy, P.H.4    Hollenberg, P.F.5    Vaz, A.D.N.6    Coon, M.J.7
  • 38
    • 0542422859 scopus 로고    scopus 로고
    • Heme Oxygenase Mechanism: Evidence for an Electrophilic, Ferric Peroxide Species
    • Ortiz de Montellano, P. R. Heme Oxygenase Mechanism: Evidence for an Electrophilic, Ferric Peroxide Species. Acc. Chem. Res. 1998, 31, 543-549.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 543-549
    • Ortiz de Montellano, P.R.1
  • 40
    • 0034821220 scopus 로고    scopus 로고
    • High-frequency (140-GHz) time domain EPR and ENDOR spectroscopy: The tyrosyl radical-diiron cofactor in ribonucleotide reductase from yeast
    • Bar, G.; Bennati, M.; Nguyen, H.-H. T.; Ge, J.; Stubbe, J.; Griffin, R. G. High-frequency (140-GHz) time domain EPR and ENDOR spectroscopy: The tyrosyl radical-diiron cofactor in ribonucleotide reductase from yeast. J. Am. Chem. Soc. 2001, 123, 3569-3576.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3569-3576
    • Bar, G.1    Bennati, M.2    Nguyen, H.-H.T.3    Ge, J.4    Stubbe, J.5    Griffin, R.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.