메뉴 건너뛰기




Volumn 45, Issue 14, 2006, Pages 4578-4592

Backbone NMR assignments and H/D exchange studies on the ferric azide- and cyanide-inhibited forms of Pseudomonas aeruginosa heme oxygenase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RESONANCE; WATER;

EID: 33645659520     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0600188     Document Type: Article
Times cited : (18)

References (69)
  • 1
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen, R., Marver, H. S., and Schmid, R. (1969) Microsomal heme oxygenase. characterization of the enzyme, J. Biol. Chem. 244, 6388-6394.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 2
    • 0031984804 scopus 로고    scopus 로고
    • Absorption of heme iron
    • Uzel, C., and Conrad, M. E. (1998) Absorption of heme iron, Semin. Hematol. 35, 27-34.
    • (1998) Semin. Hematol. , vol.35 , pp. 27-34
    • Uzel, C.1    Conrad, M.E.2
  • 3
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines, M. D. (1997) The heme oxygenase system: a regulator of second messenger gases, Annu. Rev. Pharmacol. Toxicol. 37, 517-554.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 4
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N., and Ames, B. N. (1987) Bilirubin is an antioxidant of possible physiological importance, Science 235, 1043-1046.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 5
    • 0031214204 scopus 로고    scopus 로고
    • New physiological importance of two classic residual products: Carbon monoxide and billirubin
    • Marilena, G. (1997) New physiological importance of two classic residual products: carbon monoxide and billirubin, Biochem. Mol. Med. 61, 136-142.
    • (1997) Biochem. Mol. Med. , vol.61 , pp. 136-142
    • Marilena, G.1
  • 7
    • 0031984521 scopus 로고    scopus 로고
    • Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae
    • Wilks, A., and Schmitt, M. P. (1998) Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae, J. Biol. Chem. 273, 837-841.
    • (1998) J. Biol. Chem. , vol.273 , pp. 837-841
    • Wilks, A.1    Schmitt, M.P.2
  • 8
    • 0033988059 scopus 로고    scopus 로고
    • Use of heme compounds as iron sources by pathogenic Neisseriae requires the product of the hemO gene
    • Zhu, W., Hunt, D. J., Richardson, A. R., and Stojiljkovic, I. (2000) Use of heme compounds as iron sources by pathogenic Neisseriae requires the product of the hemO gene, J. Bacteriol. 182, 439-447.
    • (2000) J. Bacteriol. , vol.182 , pp. 439-447
    • Zhu, W.1    Hunt, D.J.2    Richardson, A.R.3    Stojiljkovic, I.4
  • 9
    • 0031034090 scopus 로고    scopus 로고
    • Utilization of host iron sources by Corynebacterium diphteriae: Identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin
    • Schmitt, M. P. (1997) Utilization of host iron sources by Corynebacterium diphteriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin, J. Bacteriol. 179, 838-845.
    • (1997) J. Bacteriol. , vol.179 , pp. 838-845
    • Schmitt, M.P.1
  • 10
    • 0035688874 scopus 로고    scopus 로고
    • Homologues of Neisserial heme oxygenase in gram-negative bacteria: Degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa
    • Ratliff, M., Zhu, W., Deshmukh, R., Wilks, A., and Stojiljkovic, I. (2001) Homologues of Neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa, J. Bacteriol. 183, 6394-6403.
    • (2001) J. Bacteriol. , vol.183 , pp. 6394-6403
    • Ratliff, M.1    Zhu, W.2    Deshmukh, R.3    Wilks, A.4    Stojiljkovic, I.5
  • 11
    • 0345791519 scopus 로고    scopus 로고
    • IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus
    • Skaar, E. P., Gaspar, A. H., and Schneewind, O. (2004) IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus, J. Biol. Chem. 279, 436-443.
    • (2004) J. Biol. Chem. , vol.279 , pp. 436-443
    • Skaar, E.P.1    Gaspar, A.H.2    Schneewind, O.3
  • 12
    • 0942287210 scopus 로고    scopus 로고
    • Heme oxygenase in Candida albicans is regulated by hemoglobin and is necessary for metabolism of exogenous heme and hemoglobin to α-biliverdin
    • Pendrak, M. L., Chao, M. P., Yan, S. S., and Roberts, D. D. (2004) Heme oxygenase in Candida albicans is regulated by hemoglobin and is necessary for metabolism of exogenous heme and hemoglobin to α-biliverdin, J. Biol. Chem. 279, 3426-3433.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3426-3433
    • Pendrak, M.L.1    Chao, M.P.2    Yan, S.S.3    Roberts, D.D.4
  • 13
    • 28044471997 scopus 로고    scopus 로고
    • Identification of an Escherichia coli 0157:H7 heme oxygenase with tandem functional repeats
    • Suits, M. D., Pal, G. P., Nakatsu, K., Matte, A., Cygler, M., and Jia, Z. (2005) Identification of an Escherichia coli 0157:H7 heme oxygenase with tandem functional repeats, Proc. Natl. Acad. Sci. U.S.A. 102, 16955-16960.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 16955-16960
    • Suits, M.D.1    Pal, G.P.2    Nakatsu, K.3    Matte, A.4    Cygler, M.5    Jia, Z.6
  • 14
    • 0033609945 scopus 로고    scopus 로고
    • The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae
    • Chu, G. C., Tomita, T., Sönnichsen, F. D., Yoshida, T., and Ikeda-Saito, M. (1999) The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae, J. Biol. Chem. 274, 24490-24496.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24490-24496
    • Chu, G.C.1    Tomita, T.2    Sönnichsen, F.D.3    Yoshida, T.4    Ikeda-Saito, M.5
  • 15
    • 1642441846 scopus 로고    scopus 로고
    • The crystal structures of the ferrie and ferrous forms of the heme complex of HmuO, a heme oxyenase of Corynebacterium diphtheriae
    • Hirotsu, S., Chu, G. C., Unno, M., Lee, D.-S., Yoshida, T., Park, S.-Y., Shiro, Y., and Ikeda-Saito, M. (2004) The crystal structures of the ferrie and ferrous forms of the heme complex of HmuO, a heme oxyenase of Corynebacterium diphtheriae, J. Biol. Chem. 279, 11937-11947.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11937-11947
    • Hirotsu, S.1    Chu, G.C.2    Unno, M.3    Lee, D.-S.4    Yoshida, T.5    Park, S.-Y.6    Shiro, Y.7    Ikeda-Saito, M.8
  • 16
    • 0034461244 scopus 로고    scopus 로고
    • Degradation of heme in gram-negative bacteria: The product of the hemO gene of Neisseriae is a heme oxygenase
    • Zhu, W., Wilks, A., and Stojiljkovic, I. (2000) Degradation of heme in gram-negative bacteria: the product of the hemO gene of Neisseriae is a heme oxygenase, J. Bacteriol. 182, 6783-6790.
    • (2000) J. Bacteriol. , vol.182 , pp. 6783-6790
    • Zhu, W.1    Wilks, A.2    Stojiljkovic, I.3
  • 17
    • 0035949642 scopus 로고    scopus 로고
    • Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase
    • Schuller, D. J., Zhu, W., Stojiljkovic, I., Wilks, A., and Poulos, T. L. (2001) Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase, Biochemistry 40, 11552-11558.
    • (2001) Biochemistry , vol.40 , pp. 11552-11558
    • Schuller, D.J.1    Zhu, W.2    Stojiljkovic, I.3    Wilks, A.4    Poulos, T.L.5
  • 18
    • 0346037293 scopus 로고    scopus 로고
    • Oxidation of heme to β- atnd δ-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme
    • Caignan, G. A., Deshmukh, R., Wilks, A., Zeng, Y., Huang, H., Moënne-Loccoz, P., Bunce, R. A., Eastman, M. A., and Rivera, M. (2002) Oxidation of heme to β- and δ-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme, J. Am. Chem. Soc. 124, 14879-14892.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14879-14892
    • Caignan, G.A.1    Deshmukh, R.2    Wilks, A.3    Zeng, Y.4    Huang, H.5    Moënne-Loccoz, P.6    Bunce, R.A.7    Eastman, M.A.8    Rivera, M.9
  • 19
    • 2442496416 scopus 로고    scopus 로고
    • Structural basis for novel δ-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa
    • Friedman, J., Lad, L., Li, H., Wilks, A., and Poulos, T. L. (2004) Structural basis for novel δ-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa, Biochemistry 43, 5239-5245.
    • (2004) Biochemistry , vol.43 , pp. 5239-5245
    • Friedman, J.1    Lad, L.2    Li, H.3    Wilks, A.4    Poulos, T.L.5
  • 20
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: A common cause of persistent infection
    • Costerton, J. W., Stewart, P. S., and Greenberg, E. P. (1999) Bacterial biofilms: a common cause of persistent infection, Science 284, 1318-1322.
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 21
    • 0033955445 scopus 로고    scopus 로고
    • Genetics and regulation of two distinct haem-uptake systems, phu and has, in Pseudomonas aeruginosa
    • Ochsner, U. A., Johnson, Z., and Vasil, A. I. (2000) Genetics and regulation of two distinct haem-uptake systems, phu and has, in Pseudomonas aeruginosa. Microbiology 146, 185-198.
    • (2000) Microbiology , vol.146 , pp. 185-198
    • Ochsner, U.A.1    Johnson, Z.2    Vasil, A.I.3
  • 22
    • 0032704951 scopus 로고    scopus 로고
    • The response of Pseudomonas aeruginosa to iron: Genetics, biochemistry and virulence
    • Vasil, M. L., and Ochsner, U. A. (1999) The response of Pseudomonas aeruginosa to iron: genetics, biochemistry and virulence, Mol. Microbiol. 34, 399-413.
    • (1999) Mol. Microbiol. , vol.34 , pp. 399-413
    • Vasil, M.L.1    Ochsner, U.A.2
  • 25
    • 0037181030 scopus 로고    scopus 로고
    • Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants
    • Davydov, R., Kofman, V., Fujii, H., Yoshida, T., Ikeda-Saito, M., and Hoffman, B. M. (2002) Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants, J. Am. Chem. Soc. 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.M.6
  • 27
    • 0542422859 scopus 로고    scopus 로고
    • Heme oxygenase mechanism: Evidence for an electrophilic, ferric peroxide species
    • Ortiz de Montellano, P. R. (1998) Heme oxygenase mechanism: evidence for an electrophilic, ferric peroxide species, Acc. Chem. Res. 31, 543-549.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 543-549
    • Ortiz De Montellano, P.R.1
  • 28
    • 10644235507 scopus 로고    scopus 로고
    • Heme oxygenase, steering dioxygen activation toward heme hydroxylation
    • Rivera, M., and Zeng, Y. (2005) Heme oxygenase, steering dioxygen activation toward heme hydroxylation, J. Inorg. Biochem. 99, 337-354.
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 337-354
    • Rivera, M.1    Zeng, Y.2
  • 32
    • 0000849904 scopus 로고
    • Models of the cytochromes b. Low-spin bis-ligated (porphinato)iron(III) complexes with "unusual" molecular structures and NMR, EPR, and Mösbauer spectra
    • Safo, M. K., Gupta, G. P., Watson, C. T., Simonis, U., Walker, F. A., and Scheidt, W. R. (1992) Models of the cytochromes b. Low-spin bis-ligated (porphinato)iron(III) complexes with "unusual" molecular structures and NMR, EPR, and Mösbauer spectra, J. Am. Chem. Soc. 114, 7066-7075.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7066-7075
    • Safo, M.K.1    Gupta, G.P.2    Watson, C.T.3    Simonis, U.4    Walker, F.A.5    Scheidt, W.R.6
  • 33
    • 0034679068 scopus 로고    scopus 로고
    • - ligand field strength on the magnetochemical series relative to the spectrochemical series. Novel 1-equiv water chemistry of iron-(III) tetraphenylporphyrin complexes
    • - ligand field strength on the magnetochemical series relative to the spectrochemical series. Novel 1-equiv water chemistry of iron-(III) tetraphenylporphyrin complexes, J. Am. Chem. Soc. 122, 4660-4667.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4660-4667
    • Evans, D.R.1    Reed, C.A.2
  • 34
    • 0001165867 scopus 로고    scopus 로고
    • Nuclear Magnetic resonance of hemoproteins
    • Academic Press, San Diego, CA
    • La Mar, G. N., Satterlee, J. D., and De Ropp, J. S. (2000) Nuclear Magnetic resonance of hemoproteins, in The Porphyrin Handbook 5, pp 185-297, Academic Press, San Diego, CA.
    • (2000) The Porphyrin Handbook , vol.5 , pp. 185-297
    • La Mar, G.N.1    Satterlee, J.D.2    De Ropp, J.S.3
  • 35
    • 20444399563 scopus 로고    scopus 로고
    • Theory favors a stepwise mechanism of porphyrin degradation by a ferric hydroperoxide model of the active species of heme oxygenase
    • Kumar, D., de Visser, S. P., and Shaik, S. (2005) Theory favors a stepwise mechanism of porphyrin degradation by a ferric hydroperoxide model of the active species of heme oxygenase, J. Am. Chem. Soc. 127, 8204-8213.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8204-8213
    • Kumar, D.1    De Visser, S.P.2    Shaik, S.3
  • 37
    • 0242330799 scopus 로고    scopus 로고
    • 15N NMR spectroscopic characterization of substrate-bound, cyanide-inhibited human heme oxygenase: Water occupation of the distal cavity
    • 15N NMR spectroscopic characterization of substrate-bound, cyanide-inhibited human heme oxygenase: water occupation of the distal cavity, J. Am. Chem. Soc. 125, 13392-13403.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13392-13403
    • Li, Y.1    Syvitski, R.T.2    Auclair, K.3    Ortiz De Montellano, P.R.4    La Mar, G.N.5
  • 38
    • 3543123507 scopus 로고    scopus 로고
    • 1H NMR characterization of the solution active site of substrate-bound, cyanide-inhibited heme oxygenase from Neisseria meningitidis: Comparison to crystal structures
    • 1H NMR characterization of the solution active site of substrate-bound, cyanide-inhibited heme oxygenase from Neisseria meningitidis: comparison to crystal structures, Biochemistry 43, 10112-10126.
    • (2004) Biochemistry , vol.43 , pp. 10112-10126
    • Liu, Y.1    Zhang, X.2    Yoshida, T.3    La Mar, G.N.4
  • 39
    • 18244368735 scopus 로고    scopus 로고
    • 1H NMR characterization of the distal H-bond network and the effective axial field in the resting state, high-spin ferric, substrate-bound complex of heme oxygenase from N. meningitidis
    • 1H NMR characterization of the distal H-bond network and the effective axial field in the resting state, high-spin ferric, substrate-bound complex of heme oxygenase from N. meningitidis, J. Am. Chem. Soc. 127, 6409-6422.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6409-6422
    • Liu, Y.1    Zhang, X.2    Yoshida, T.3    La Mar, G.N.4
  • 40
    • 0028889024 scopus 로고
    • Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative [2Fe-2S] ferredoxin
    • Cheng, H., Westler, W. M., Xia, B., Oh, B.-H., and Markley, J. L. (1995) Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative [2Fe-2S] ferredoxin, Arch. Biochem. Biophys. 316 619-634.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 619-634
    • Cheng, H.1    Westler, W.M.2    Xia, B.3    Oh, B.-H.4    Markley, J.L.5
  • 41
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, W., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, W.4    Pfeifer, J.5    Bax, A.6
  • 42
    • 33645658931 scopus 로고    scopus 로고
    • Goddard, T. D., and Kneller, D. G. Sparky 3, University of California, San Francisco, CA
    • Goddard, T. D., and Kneller, D. G. Sparky 3, University of California, San Francisco, CA.
  • 44
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity, J. Am. Chem. Soc. 114, 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 46
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A., and Nielsen, S. O. (1966) Hydrogen exchange in proteins, Adv. Protein Chem. 21, 288-380.
    • (1966) Adv. Protein Chem. , vol.21 , pp. 288-380
    • Hvidt, A.1    Nielsen, S.O.2
  • 48
    • 2442645409 scopus 로고    scopus 로고
    • Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: Implications for heme oxygenase function
    • Unno, M., Matsui, T., Chu, G. C., Couture, M., Yoshida, T., Rousseau, D. L., Olson, J. S., and Ikeda-Saito, M. (2004) Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function, J. Biol. Chem. 279, 21055-21061.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21055-21061
    • Unno, M.1    Matsui, T.2    Chu, G.C.3    Couture, M.4    Yoshida, T.5    Rousseau, D.L.6    Olson, J.S.7    Ikeda-Saito, M.8
  • 51
    • 0035743297 scopus 로고    scopus 로고
    • Use of carbonyl chemical shift to relieve degeneracies in triple-resonance assignment experiments
    • Sayers, E. W., and Torchia, D. A. (2001) Use of carbonyl chemical shift to relieve degeneracies in triple-resonance assignment experiments, J. Magn. Reson. 153, 246-253.
    • (2001) J. Magn. Reson. , vol.153 , pp. 246-253
    • Sayers, E.W.1    Torchia, D.A.2
  • 52
    • 2342512067 scopus 로고    scopus 로고
    • Strategy for the study of paramagnetic proteins with slow electronic relaxation rates by NMR spectroscopy: Application to oxidized human [2Fe-2S] ferredoxin
    • Machonkin, T. E., Westler, W. M., and Markley, J. L. (2004) Strategy for the study of paramagnetic proteins with slow electronic relaxation rates by NMR spectroscopy: application to oxidized human [2Fe-2S] ferredoxin, J. Am. Chem. Soc. 126, 5413-5426.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5413-5426
    • Machonkin, T.E.1    Westler, W.M.2    Markley, J.L.3
  • 53
    • 0032519626 scopus 로고    scopus 로고
    • A substrate-induced change in the stereospecificity of the serine-hydroxymethyltransferase-catalyzed exchange of the α-protons of amino acids
    • Fitzpatrick, T. B., and Malthouse, J. P. G. (1998) A substrate-induced change in the stereospecificity of the serine-hydroxymethyltransferase-catalyzed exchange of the α-protons of amino acids, Eur. J. Biochem. 252, 113-117.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 113-117
    • Fitzpatrick, T.B.1    Malthouse, J.P.G.2
  • 55
    • 0001956446 scopus 로고
    • NMR methodology for paramagnetic proteins
    • La Mar, G. N., and de Ropp, J. S. (1993) NMR methodology for paramagnetic proteins, Biol. Magn. Reson. 12, 1-78.
    • (1993) Biol. Magn. Reson. , vol.12 , pp. 1-78
    • La Mar, G.N.1    De Ropp, J.S.2
  • 58
    • 2442444243 scopus 로고    scopus 로고
    • Mixed regioselectivity in the Arg-177 mutants of Corynebacterium diphtheriae heme oxygenase as a consequence of in-plane heme disorder
    • Zeng, Y., Deshmukh, R., Caignan, G. A., Bunce, R. A., Rivera, M., and Wilks, A. (2004) Mixed regioselectivity in the Arg-177 mutants of Corynebacterium diphtheriae heme oxygenase as a consequence of in-plane heme disorder, Biochemistry 43, 5222-5238.
    • (2004) Biochemistry , vol.43 , pp. 5222-5238
    • Zeng, Y.1    Deshmukh, R.2    Caignan, G.A.3    Bunce, R.A.4    Rivera, M.5    Wilks, A.6
  • 59
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. P. (2002) Mapping protein-protein interactions in solution by NMR spectroscopy, Biochemistry 41, 1-7.
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.P.1
  • 60
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart, D. S., and Sykes, B. D. (1994) Chemical shifts as a tool for structure determination, Methods Enzymol. 239, 363.
    • (1994) Methods Enzymol. , vol.239 , pp. 363
    • Wishart, D.S.1    Sykes, B.D.2
  • 61
    • 0037709372 scopus 로고    scopus 로고
    • Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp40AIa mutant of human heme oxygenase-1: Catalytic implications
    • Lad, L., Wang, J., Li, H., Friedman, J., Bhaskar, B., Ortiz de Montellano, P. R., and Poulos, T. L. (2003) Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp40AIa mutant of human heme oxygenase-1: catalytic implications, J. Mol. Biol. 330, 527-538.
    • (2003) J. Mol. Biol. , vol.330 , pp. 527-538
    • Lad, L.1    Wang, J.2    Li, H.3    Friedman, J.4    Bhaskar, B.5    Ortiz De Montellano, P.R.6    Poulos, T.L.7
  • 62
    • 0037073478 scopus 로고    scopus 로고
    • The solution structure of the recombinant hemoglobin from the Cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state
    • Falzone, J. C., Vu, B. C., Scott, N. L., and Lecomte, J. T. J. (2002) The solution structure of the recombinant hemoglobin from the Cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state, J. Mol. Biol. 324, 1015-1029.
    • (2002) J. Mol. Biol. , vol.324 , pp. 1015-1029
    • Falzone, J.C.1    Vu, B.C.2    Scott, N.L.3    Lecomte, J.T.J.4
  • 63
    • 0032550615 scopus 로고    scopus 로고
    • 15N NMR chemical shifts in iron-sulfur proteins as determined by comparison of experimental data with hybrid density functional calculations
    • 15N NMR chemical shifts in iron-sulfur proteins as determined by comparison of experimental data with hybrid density functional calculations, J. Am. Chem. Soc. 120, 4806-4814.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4806-4814
    • Wilkens, S.J.1    Xia, B.2    Weinhold, F.3    Markley, J.L.4    Westler, W.M.5
  • 64
    • 0001601463 scopus 로고    scopus 로고
    • 15N chemical shifts in Clostridium pasteurianum rubredoxin by fermi-contact effects through hydrogen bonds
    • 15N chemical shifts in Clostridium pasteurianum rubredoxin by fermi-contact effects through hydrogen bonds, J. Am. Chem. Soc. 120, 4893-4894.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4893-4894
    • Xia, B.1    Wilkens, S.J.2    Westler, W.M.3    Markley, J.L.4
  • 66
    • 0027998288 scopus 로고
    • Heme oxygenase (HO-1): Evidence for electrophilic oxygen addition to the porphyrin ring in the formation of α-meso-hydroxyheme
    • Wilks, A., Torpey, J., and Ortiz de Montellano, P. R. (1994) Heme oxygenase (HO-1): evidence for electrophilic oxygen addition to the porphyrin ring in the formation of α-meso-hydroxyheme, J. Biol. Chem. 269, 29553-29556.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29553-29556
    • Wilks, A.1    Torpey, J.2    Ortiz De Montellano, P.R.3
  • 67
    • 1642307574 scopus 로고    scopus 로고
    • How heme metabolism occurs in heme oxygenase: Computational study of oxygen-donation ability of the oxo and hydroperoxo species
    • Kamachi, T., Shestakov, A. F., Yoshizawa, K. (2004) How heme metabolism occurs in heme oxygenase: computational study of oxygen-donation ability of the oxo and hydroperoxo species, J. Am. Chem. Soc. 126, 3672-3673.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3672-3673
    • Kamachi, T.1    Shestakov, A.F.2    Yoshizawa, K.3
  • 68
    • 0033579110 scopus 로고    scopus 로고
    • EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: Mutation-induced changes in the proton delivery system
    • Davydov, R., Macdonald, I. D. G., Makris, T. M., Sligar, S. G., and Hoffman, B. M. (1999) EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: mutation-induced changes in the proton delivery system, J. Am. Chem. Soc. 121, 10654-10655.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10654-10655
    • Davydov, R.1    Macdonald, I.D.G.2    Makris, T.M.3    Sligar, S.G.4    Hoffman, B.M.5
  • 69
    • 23044434960 scopus 로고    scopus 로고
    • Water-assisted mechanism for heme metabolism
    • Kamachi, T., and Yoshizawa, K. (2005) Water-assisted mechanism for heme metabolism, J. Am. Chem. Soc. 127, 10686-10692.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10686-10692
    • Kamachi, T.1    Yoshizawa, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.