메뉴 건너뛰기




Volumn 288, Issue 48, 2013, Pages 34443-34458

Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: X-ray crystallography and molecular dynamics investigation

Author keywords

[No Author keywords available]

Indexed keywords

CORYNEBACTERIUM DIPHTHERIAE; ENZYME ACTIVE SITES; HELICAL CONFORMATION; HEME DEGRADATION; HEME OXYGENASES; HYDROGEN BOND NETWORKS; LATTER COMPLEXES; SUBSTRATE-BOUND;

EID: 84889045759     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.486936     Document Type: Article
Times cited : (15)

References (63)
  • 1
    • 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
  • 2
    • 0015501157 scopus 로고
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
    • Schacter, B. A., Nelson, E. B., Marver, H. S., Masters, B. S. (1972) Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system. J. Biol. Chem. 247, 3601-3607
    • (1972) J. Biol. Chem , vol.247 , pp. 3601-3607
    • Schacter, B.A.1    Nelson, E.B.2    Marver, H.S.3    Masters, B.S.4
  • 3
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss, K. D., and Tonegawa, S. (1997) Heme oxygenase 1 is required for mammalian iron reutilization. Proc. Natl. Acad. Sci. U.S.A. 94, 10919- 10924
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 5
    • 84864285556 scopus 로고    scopus 로고
    • H2S signaling through protein sulfhydration and beyond
    • Paul, B. D., and Snyder, S. H. (2012) H2S signaling through protein sulfhydration and beyond. Nat. Rev. Mol. Cell Biol. 13, 499-507
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 499-507
    • Paul, B.D.1    Snyder, S.H.2
  • 6
    • 0037898944 scopus 로고    scopus 로고
    • Autocatalytic radical reactions in physiological prosthetic heme modification
    • Colas, C., and Ortiz de Montellano, P. R. (2003) Autocatalytic radical reactions in physiological prosthetic heme modification. Chem. Rev. 103, 2305-2332
    • (2003) Chem. Rev , vol.103 , pp. 2305-2332
    • Colas, C.1    De Montellano, O.2    Ortiz De Montellano, P.R.3
  • 7
    • 34249826339 scopus 로고    scopus 로고
    • Heme and virulence: How bacterial pathogens regulate, transport, and utilize heme
    • Wilks, A., and Burkhard, K. A. (2007) Heme and virulence: How bacterial pathogens regulate, transport, and utilize heme. Nat. Prod. Rep. 24, 511-522
    • (2007) Nat. Prod. Rep , vol.24 , pp. 511-522
    • Wilks, A.1    Burkhard, K.A.2
  • 8
    • 78649921851 scopus 로고    scopus 로고
    • Overcoming the heme paradox: Heme toxicity and tolerance in bacterial pathogens
    • Anzaldi, L. L., and Skaar, E. P. (2010) Overcoming the heme paradox: Heme toxicity and tolerance in bacterial pathogens. Infect. Immun. 78, 4977-4989
    • (2010) Infect. Immun , vol.78 , pp. 4977-4989
    • Anzaldi, L.L.1    Skaar, E.P.2
  • 10
    • 84875981467 scopus 로고    scopus 로고
    • A new way to degrade heme: The Mycobacterium tuberculosis enzymeMhuDcatalyzes heme degradation without generating CO
    • Nambu, S., Matsui, T., Goulding, C. W., Takahashi, S., and Ikeda-Saito, M. (2013) A new way to degrade heme: The Mycobacterium tuberculosis enzymeMhuDcatalyzes heme degradation without generating CO. J. Biol. Chem. 288, 10101-10109
    • (2013) J. Biol. Chem , vol.288 , pp. 10101-10109
    • Nambu, S.1    Matsui, T.2    Goulding, C.W.3    Takahashi, S.4    Ikeda-Saito, M.5
  • 11
    • 84877315338 scopus 로고    scopus 로고
    • Heme degradation by Staphylococcus aureus IsdG and isdI liberates formaldehyde rather than carbon monoxide
    • Matsui, T., Nambu, S., Ono, Y., Goulding, C. W., Tsumoto, K., and Ikeda- Saito, M. (2013) Heme degradation by Staphylococcus aureus IsdG and isdI liberates formaldehyde rather than carbon monoxide. Biochemistry 52, 3025-3027
    • (2013) Biochemistry , vol.52 , pp. 3025-3027
    • Matsui, T.1    Nambu, S.2    Ono, Y.3    Goulding, C.W.4    Tsumoto, K.5    Ikeda- Saito, M.6
  • 12
    • 0031034090 scopus 로고    scopus 로고
    • Utilization of host iron sources by Corynebacterium diphtheriae: 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 diphtheriae: 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
  • 13
    • 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
  • 14
    • 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
  • 15
    • 0031984521 scopus 로고    scopus 로고
    • Expression and characterization of a heme oxygenase (HmuO) from Corynebacterium diphtheriae: Iron acquisition requires oxidative cleavage of the heme macrocycle
    • Wilks, A., and Schmitt, M. P. (1998) Expression and characterization of a heme oxygenase (HmuO) from Corynebacterium diphtheriae: Iron acquisition requires oxidative cleavage of the heme macrocycle. J. Biol. Chem. 273, 837-841
    • (1998) J. Biol. Chem , vol.273 , pp. 837-841
    • Wilks, A.1    Schmitt, M.P.2
  • 16
    • 0033597730 scopus 로고    scopus 로고
    • Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (HmuO) from Corynebacterium diphtheriae
    • Chu, G. C., Katakura, K., Zhang, X., Yoshida, T., and Ikeda-Saito, M. (1999) Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (HmuO) from Corynebacterium diphtheriae. J. Biol. Chem. 274, 21319-21325
    • (1999) J. Biol. Chem , vol.274 , pp. 21319-21325
    • Chu, G.C.1    Katakura, K.2    Zhang, X.3    Yoshida, T.4    Ikeda-Saito, M.5
  • 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-1
    • 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-1. 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
    • 1642441846 scopus 로고    scopus 로고
    • The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase 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 ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase 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
  • 19
    • 2442496416 scopus 로고    scopus 로고
    • Structural basis for novel δ-regioselective heme oxygenation in 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 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
  • 21
    • 0036672234 scopus 로고    scopus 로고
    • Heme oxygenase: Evolution, structure, and mechanism
    • Wilks, A. (2002) Heme oxygenase: Evolution, structure, and mechanism. Antioxid. Redox Signal. 4, 603-614
    • (2002) Antioxid. Redox Signal , vol.4 , pp. 603-614
    • Wilks, A.1
  • 22
    • 34249803283 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of heme oxygenase
    • Unno, M., Matsui, T., and Ikeda-Saito, M. (2007) Structure and catalytic mechanism of heme oxygenase. Nat. Prod. Rep. 24, 553-570
    • (2007) Nat. Prod. Rep , vol.24 , pp. 553-570
    • Unno, M.1    Matsui, T.2    Ikeda-Saito, M.3
  • 23
    • 77249168703 scopus 로고    scopus 로고
    • Heme oxygenase reveals its strategy for catalyzing three successive oxygenation reactions
    • Matsui, T., Unno, M., and Ikeda-Saito, M. (2010) Heme oxygenase reveals its strategy for catalyzing three successive oxygenation reactions. Acc. Chem. Res. 43, 240-247
    • (2010) Acc. Chem. Res , vol.43 , pp. 240-247
    • Matsui, T.1    Unno, M.2    Ikeda-Saito, M.3
  • 24
    • 77950992025 scopus 로고    scopus 로고
    • Dioxygen activation for self-degradation of heme: Reaction mechanism and regulation of heme oxygenase
    • Matsui, T., Iwasaki, M., Sugiyama, R., Unno, M., and Ikeda-Saito, M. (2010) Dioxygen activation for self-degradation of heme: Reaction mechanism and regulation of heme oxygenase. Inorg. Chem. 49, 3602-3609
    • (2010) Inorg. Chem , vol.49 , pp. 3602-3609
    • Matsui, T.1    Iwasaki, M.2    Sugiyama, R.3    Unno, M.4    Ikeda-Saito, M.5
  • 25
    • 77956626980 scopus 로고    scopus 로고
    • Enzymatic ring-opening mechanism of verdoheme by the heme oxygenase: A combined x-ray crystallography and QM/MM study
    • Lai, W., Chen, H., Matsui, T., Omori, K., Unno, M., Ikeda-Saito, M., and Shaik, S. (2010) Enzymatic ring-opening mechanism of verdoheme by the heme oxygenase: A combined x-ray crystallography and QM/MM study. J. Am. Chem. Soc. 132, 12960-12970
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 12960-12970
    • Lai, W.1    Chen, H.2    Matsui, T.3    Omori, K.4    Unno, M.5    Ikeda-Saito, M.6    Shaik, S.7
  • 26
    • 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
  • 27
    • 0017900548 scopus 로고
    • Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system
    • Yoshida, T., and Kikuchi, G. (1978) Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system. J. Biol. Chem. 253, 4230-4236
    • (1978) J. Biol. Chem , vol.253 , pp. 4230-4236
    • Yoshida, T.1    Kikuchi, G.2
  • 28
    • 84863725870 scopus 로고    scopus 로고
    • Crystallographic studies of heme oxygenase complexed with an unstable reaction intermediate, verdoheme
    • Unno, M., Matsui, T., and Ikeda-Saito, M. (2012) Crystallographic studies of heme oxygenase complexed with an unstable reaction intermediate, verdoheme. J. Inorg. Biochem. 113, 102-109
    • (2012) J. Inorg. Biochem , vol.113 , pp. 102-109
    • Unno, M.1    Matsui, T.2    Ikeda-Saito, M.3
  • 29
    • 0037062587 scopus 로고    scopus 로고
    • Crystal structure of rat apo-heme oxygenase- 1 (HO-1): Mechanism of heme binding in HO-1 inferred from structural comparison of the apo and heme complex forms
    • Sugishima, M., Sakamoto, H., Kakuta, Y., Omata, Y., Hayashi, S., Noguchi, M., and Fukuyama, K. (2002) Crystal structure of rat apo-heme oxygenase- 1 (HO-1): Mechanism of heme binding in HO-1 inferred from structural comparison of the apo and heme complex forms. Biochemistry 41, 7293-7300
    • (2002) Biochemistry , vol.41 , pp. 7293-7300
    • Sugishima, M.1    Sakamoto, H.2    Kakuta, Y.3    Omata, Y.4    Hayashi, S.5    Noguchi, M.6    Fukuyama, K.7
  • 32
    • 37049108250 scopus 로고
    • Crystal and molecular structure of biliverdin dimethyl ester
    • Sheldrick, W. S. (1976) Crystal and molecular structure of biliverdin dimethyl ester. J. Chem. Soc. Perkin Trans. 2, 1453-1462
    • (1976) J. Chem. Soc. Perkin Trans , vol.2 , pp. 1453-1462
    • Sheldrick, W.S.1
  • 33
    • 0028958953 scopus 로고
    • Structure determination of the biliverdin apomyoglobin complex: Crystal structure analysis of two crystal forms at 1.4 and 1.5 Å resolution
    • Wagner, U.G., Müller, N., Schmitzberger, W., Falk H., and Kratky, C. (1995) Structure determination of the biliverdin apomyoglobin complex: Crystal structure analysis of two crystal forms at 1.4 and 1.5 Å resolution. J. Mol. Biol. 247, 326-337
    • (1995) J. Mol. Biol , vol.247 , pp. 326-337
    • Wagner, U.G.1    Müller, N.2    Schmitzberger, W.3    Falk, H.4    Kratky, C.5
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No 4
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
  • 38
    • 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. E., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A Found. Crystallogr. 47, 110-119
    • (1991) Acta Crystallogr. Sect. A Found. Crystallogr , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.E.3    Kjeldgaard, M.4
  • 39
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones, T. A. (1978) A graphics model building and refinement system for macromolecules. J. Appl. Cryst. 11, 268-272
    • (1978) J. Appl. Cryst , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 42
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf, R. M. (1999) Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr.DBiol. Crystallogr. 55, 938-940
    • (1999) Acta Crystallogr.DBiol. Crystallogr , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 43
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277, 505-524
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 46
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics, and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman, D. A., Case, D. A., Caldwell, J. W., Ross, W. S., Cheatham, T. E., III, Debolt, S., Ferguson, D., Seibel, G., and Kollman, P. A. (1995) AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics, and free energy calculations to simulate the structural and energetic properties of molecules. Comput. Phys. Commun. 91, 1-41
    • (1995) Comput. Phys. Commun , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham III, T.E.5    Debolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.A.9
  • 48
    • 73349098763 scopus 로고    scopus 로고
    • A collective variable for the efficient exploration of protein β-sheet structures: Application to SH3 and GB1
    • Pietrucci, F., and Laio, A. (2009) A collective variable for the efficient exploration of protein β-sheet structures: Application to SH3 and GB1. J. Chem. Theory Comput. 5, 2197-2201
    • (2009) J. Chem. Theory Comput , vol.5 , pp. 2197-2201
    • Pietrucci, F.1    Laio, A.2
  • 49
    • 77955659803 scopus 로고    scopus 로고
    • Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: Pertinence for determining magnetic axes in paramagnetic substrate complexes
    • Du, Z., Unno, M., Matsui, T., Ikeda-Saito, M., and La Mar, G. N. (2010) Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: Pertinence for determining magnetic axes in paramagnetic substrate complexes. J. Inorg. Biochem. 104, 1063-1070
    • (2010) J. Inorg. Biochem , vol.104 , pp. 1063-1070
    • Du, Z.1    Unno, M.2    Matsui, T.3    Ikeda-Saito, M.4    La Mar, G.N.5
  • 50
    • 50449105242 scopus 로고    scopus 로고
    • Use of normal modes for structural modeling of proteins: The case study of rat heme oxygenase 1
    • Maréchal, J.-D., and Perahia, D. (2008) Use of normal modes for structural modeling of proteins: The case study of rat heme oxygenase 1. Eur. Biophys. J. 37, 1157-1165
    • (2008) Eur. Biophys. J. , vol.37 , pp. 1157-1165
    • Maréchal, J.-D.1    Perahia, D.2
  • 51
    • 38049144525 scopus 로고    scopus 로고
    • Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2
    • Bianchetti, C. M., Yi, L., Ragsdale, S. W., and Phillips, G. N., Jr. (2007) Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. J. Biol. Chem. 282, 37624-37631
    • (2007) J. Biol. Chem , vol.282 , pp. 37624-37631
    • Bianchetti, C.M.1    Yi, L.2    Ragsdale, S.W.3    Phillips Jr., G.N.4
  • 52
    • 0037470161 scopus 로고    scopus 로고
    • Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae
    • Li, Y., Syvitski, R. T., Chu, G. C., Ikeda-Saito, M., and Mar, G. N. (2003) Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae. J. Biol. Chem. 278, 6651- 6663
    • (2003) J. Biol. Chem , vol.278 , pp. 6651-6663
    • Li, Y.1    Syvitski, R.T.2    Chu, G.C.3    Ikeda-Saito, M.4    Mar, G.N.5
  • 53
    • 0041355223 scopus 로고    scopus 로고
    • Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate: Conformational change of the distal helix during the heme cleavage reaction
    • Sugishima, M., Sakamoto, H., Higashimoto, Y., Noguchi, M., and Fukuyama. (2003) Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate: Conformational change of the distal helix during the heme cleavage reaction. J. Biol. Chem. 278, 32352-32358
    • (2003) J. Biol. Chem , vol.278 , pp. 32352-32358
    • Sugishima, M.1    Sakamoto, H.2    Higashimoto, Y.3    Noguchi, M.4    Fukuyama5
  • 55
    • 4043105583 scopus 로고    scopus 로고
    • Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity
    • Xu, X., Zhao, J., Xu, Z., Peng, B., Huang, Q., Arnold, E., and Ding, J. (2004) Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity. J. Biol. Chem. 279, 33946-33957
    • (2004) J. Biol. Chem , vol.279 , pp. 33946-33957
    • Xu, X.1    Zhao, J.2    Xu, Z.3    Peng, B.4    Huang, Q.5    Arnold, E.6    Ding, J.7
  • 56
    • 84865766450 scopus 로고    scopus 로고
    • Structural basis for the transcriptional regulation of heme homeostasis in Lactococcus lactis
    • Sawai, H., Yamanaka, M., Sugimoto, H., Shiro, Y., and Aono, S. (2012) Structural basis for the transcriptional regulation of heme homeostasis in Lactococcus lactis. J. Biol. Chem. 287, 30755-30768
    • (2012) J. Biol. Chem , vol.287 , pp. 30755-30768
    • Sawai, H.1    Yamanaka, M.2    Sugimoto, H.3    Shiro, Y.4    Aono, S.5
  • 57
    • 0034128270 scopus 로고    scopus 로고
    • Corynebacterium diphtheriae genes required for acquisition of iron from haemin and haemoglobin are homologous to ABC haemin transporters
    • Drazek, E. S., Hammack, C. A., and Schmitt, M. P. (2000) Corynebacterium diphtheriae genes required for acquisition of iron from haemin and haemoglobin are homologous to ABC haemin transporters. Mol. Microbiol. 36, 68-84
    • (2000) Mol. Microbiol , vol.36 , pp. 68-84
    • Drazek, E.S.1    Hammack, C.A.2    Schmitt, M.P.3
  • 58
    • 65249145115 scopus 로고    scopus 로고
    • HtaA is an iron-regulated hemin binding protein involved in the utilization of heme iron in Corynebacterium diphtheriae
    • Allen, C. E., and Schmitt, M. P. (2009) HtaA is an iron-regulated hemin binding protein involved in the utilization of heme iron in Corynebacterium diphtheriae. J. Bacteriol. 191, 2638-2648
    • (2009) J. Bacteriol , vol.191 , pp. 2638-2648
    • Allen, C.E.1    Schmitt, M.P.2
  • 59
    • 33749010088 scopus 로고    scopus 로고
    • The mechanism of heme transfer from the cytoplasmic heme binding protein PhuS to the δ-regioselective heme oxygenase of Pseudomonas aeruginosa
    • Bhakta, M. N., and Wilks, A. (2006) The mechanism of heme transfer from the cytoplasmic heme binding protein PhuS to the δ-regioselective heme oxygenase of Pseudomonas aeruginosa. Biochemistry 45, 11642-11649
    • (2006) Biochemistry , vol.45 , pp. 11642-11649
    • Bhakta, M.N.1    Wilks, A.2
  • 60
    • 84861556687 scopus 로고    scopus 로고
    • Metabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the ironregulated heme oxygenase (HemO)
    • Barker, K. D., Barkovits, K., and Wilks, A. (2012) Metabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the ironregulated heme oxygenase (HemO). J. Biol. Chem. 287, 18342-18350
    • (2012) J. Biol. Chem , vol.287 , pp. 18342-18350
    • Barker, K.D.1    Barkovits, K.2    Wilks, A.3
  • 61
    • 33846050557 scopus 로고    scopus 로고
    • Cryoradiolytic reduction of crystalline heme proteins: Analysis by UV-Vis spectroscopy and x-ray crystallography
    • Beitlich, T., Kühnel, K., Schulze-Briese, C., Shoeman, R. L., and Schlichting, I. (2007) Cryoradiolytic reduction of crystalline heme proteins: Analysis by UV-Vis spectroscopy and x-ray crystallography. J. Synchrotron Radiat. 14, 11-23
    • (2007) J. Synchrotron Radiat , vol.14 , pp. 11-23
    • Beitlich, T.1    Kühnel, K.2    Schulze-Briese, C.3    Shoeman, R.L.4    Schlichting, I.5
  • 62
    • 0040141555 scopus 로고    scopus 로고
    • Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1
    • Liu, Y., and Ortiz de Montellano, P. R. (2000) Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1. J. Biol. Chem. 275, 5297-5307
    • (2000) J. Biol. Chem , vol.275 , pp. 5297-5307
    • Liu, Y.1    Ortiz De Montellano, P.R.2
  • 63
    • 0038165531 scopus 로고    scopus 로고
    • The binding sites on human heme oxygenase-1 for cytochrome P450 reductase and biliverdin reductase
    • Wang, J., and de Montellano, P. R. (2003) The binding sites on human heme oxygenase-1 for cytochrome P450 reductase and biliverdin reductase. J. Biol. Chem. 278, 20069-20076
    • (2003) J. Biol. Chem , vol.278 , pp. 20069-20076
    • Wang, J.1    De Montellano, P.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.