메뉴 건너뛰기




Volumn 341, Issue 1, 2004, Pages 7-13

CO-trapping site in heme oxygenase revealed by photolysis of its CO-bound heme complex: Mechanism of escaping from product inhibition

Author keywords

CO heme HO, heme HO bound to carbon monoxide; cryo trapped structure; heme oxygenase; heme HO, HO in complex with heme; HO, heme oxygenase; hydrophobic cavity; photolysis of carbon monoxide; product inhibition; verdoheme HO, HO in complex with verdoheme

Indexed keywords

CARBON MONOXIDE; HEME; HEME OXYGENASE; IRON; XENON;

EID: 4143105792     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.048     Document Type: Article
Times cited : (19)

References (37)
  • 1
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • Tenhunen R., Marver H.S., Schmid R. The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc. Natl Acad. Sci. USA. 61:1968;748-755
    • (1968) Proc. Natl Acad. Sci. USA , vol.61 , pp. 748-755
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 2
    • 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., Fukuyama K. 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. 278:2003;32352-32358
    • (2003) J. Biol. Chem. , vol.278 , pp. 32352-32358
    • Sugishima, M.1    Sakamoto, H.2    Higashimoto, Y.3    Noguchi, M.4    Fukuyama, K.5
  • 3
    • 0036775158 scopus 로고    scopus 로고
    • Heme oxygenase-1: Redox regulation and role in the hepatic response to oxidative stress
    • Bauer M., Bauer I. Heme oxygenase-1: redox regulation and role in the hepatic response to oxidative stress. Antioxid. Redox. Signal. 4:2002;749-758
    • (2002) Antioxid. Redox. Signal. , vol.4 , pp. 749-758
    • Bauer, M.1    Bauer, I.2
  • 4
    • 0035949667 scopus 로고    scopus 로고
    • Neural roles for heme oxygenase: Contrasts to nitric oxide synthase
    • Barañano D.E., Snyder S.H. Neural roles for heme oxygenase: contrasts to nitric oxide synthase. Proc. Natl Acad. Sci. USA. 98:2001;10996-11002
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10996-11002
    • Barañano, D.E.1    Snyder, S.H.2
  • 5
    • 0034652357 scopus 로고    scopus 로고
    • Carbon monoxide and nitric oxide as coneurotransmitters in the enteric nervous system: Evidence from genomic deletion of biosynthetic enzymes
    • Xue L., Farrugia G., Miller S.M., Ferris C.D., Snyder S.H., Szurszewski J.H. Carbon monoxide and nitric oxide as coneurotransmitters in the enteric nervous system: evidence from genomic deletion of biosynthetic enzymes. Proc. Natl Acad. Sci. USA. 97:2000;1851-1855
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1851-1855
    • Xue, L.1    Farrugia, G.2    Miller, S.M.3    Ferris, C.D.4    Snyder, S.H.5    Szurszewski, J.H.6
  • 6
    • 1042263983 scopus 로고    scopus 로고
    • Regulation of gonadotrophin-releasing hormone (GnRH) secretion by heme molecules: A regulatory role for carbon monoxide?
    • Lamar C.A., Mahesh V.B., Brann D.W. Regulation of gonadotrophin-releasing hormone (GnRH) secretion by heme molecules: a regulatory role for carbon monoxide? Endocrinology. 137:1996;790-793
    • (1996) Endocrinology , vol.137 , pp. 790-793
    • Lamar, C.A.1    Mahesh, V.B.2    Brann, D.W.3
  • 7
    • 0000980456 scopus 로고    scopus 로고
    • The role of carbon monoxide in the regulation of neuroendocrine function
    • Mancuso C., Preziosi P., Grossman A.B., Navarra P. The role of carbon monoxide in the regulation of neuroendocrine function. Neuroimmunomodulation. 4:1997;225-229
    • (1997) Neuroimmunomodulation , vol.4 , pp. 225-229
    • Mancuso, C.1    Preziosi, P.2    Grossman, A.B.3    Navarra, P.4
  • 8
    • 4243550127 scopus 로고    scopus 로고
    • Heme oxygenase/carbon monoxide signaling pathways: Regulation and functional significance
    • Ryter S.W., Otterbein L.E., Morse D., Choi A.M. Heme oxygenase/carbon monoxide signaling pathways: regulation and functional significance. Mol. Cell. Biochem. 234-235:2002;249-263
    • (2002) Mol. Cell. Biochem. , vol.234-235 , pp. 249-263
    • Ryter, S.W.1    Otterbein, L.E.2    Morse, D.3    Choi, A.M.4
  • 9
    • 0019332526 scopus 로고
    • Oxygenated form of heme·heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex
    • Yoshida T., Noguchi M., Kikuchi G. Oxygenated form of heme·heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex. J. Biol. Chem. 255:1980;4418-4420
    • (1980) J. Biol. Chem. , vol.255 , pp. 4418-4420
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3
  • 10
    • 35448942011 scopus 로고    scopus 로고
    • Heme oxygenase structure and function
    • (Sykes, A. G., ed.), Academic Press, San Diego.
    • Ortiz de Montellano, P. R. & Wilks, A. (2001). Heme oxygenase structure and function. Advances in Inorganic Chemistry (Sykes, A. G., ed.), vol. 51, pp. 359-407, Academic Press, San Diego.
    • (2001) Advances in Inorganic Chemistry , vol.51 , pp. 359-407
    • Ortiz De Montellano, P.R.1    Wilks, A.2
  • 11
    • 0040141555 scopus 로고    scopus 로고
    • Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1
    • Liu Y., Ortiz de Montellano P.R. Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1. J. Biol. Chem. 275:2000;5297-5307
    • (2000) J. Biol. Chem. , vol.275 , pp. 5297-5307
    • Liu, Y.1    Ortiz De Montellano, P.R.2
  • 13
    • 0019166680 scopus 로고
    • A new intermediate of heme degradation catalyzed by the heme oxygenase system
    • Yoshida T., Noguchi M., Kikuchi G. A new intermediate of heme degradation catalyzed by the heme oxygenase system. J. Biochem. (Tokyo). 88:1980;557-563
    • (1980) J. Biochem. (Tokyo) , vol.88 , pp. 557-563
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3
  • 19
    • 0028519126 scopus 로고
    • Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K
    • Teng T.Y., Šrajer V., Moffat K. Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nature Struct. Biol. 1:1994;701-705
    • (1994) Nature Struct. Biol. , vol.1 , pp. 701-705
    • Teng, T.Y.1    Šrajer, V.2    Moffat, K.3
  • 20
    • 0038472361 scopus 로고    scopus 로고
    • Direct observation of photolysis-induced tertiary structural changes in hemoglobin
    • Adachi S., Park S.Y., Tame J.R., Shiro Y., Shibayama N. Direct observation of photolysis-induced tertiary structural changes in hemoglobin. Proc. Natl Acad. Sci. USA. 100:2003;7039-7044
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 7039-7044
    • Adachi, S.1    Park, S.Y.2    Tame, J.R.3    Shiro, Y.4    Shibayama, N.5
  • 21
    • 10544231457 scopus 로고    scopus 로고
    • Photolysis of the carbon monoxide complex of myoglobin: Nanosecond time-resolved crystallography
    • Šrajer V., Teng T., Ursby T., Pradervand C., Ren Z., Adachi S., et al. Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography. Science. 274:1996;1726-1729
    • (1996) Science , vol.274 , pp. 1726-1729
    • Šrajer, V.1    Teng, T.2    Ursby, T.3    Pradervand, C.4    Ren, Z.5    Adachi, S.6
  • 24
    • 1642441846 scopus 로고    scopus 로고
    • The crystal structures of the ferric and ferrous forms of the heme complex of Hmu O, a heme oxygenase of Corynebacterium diphtheriae
    • Hirotsu S., Chu G.C., Unno M., Lee D.S., Yoshida T., Park S.Y., et al. The crystal structures of the ferric and ferrous forms of the heme complex of Hmu O, a heme oxygenase of Corynebacterium diphtheriae. J. Biol. Chem. 279:2004;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
  • 26
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9 Å
    • Tilton R.F. Jr, Kuntz I.D. Jr, Petsko G.A. Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 Å Biochemistry. 23:1984;2849-2857
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton Jr., R.F.1    Kuntz Jr., I.D.2    Petsko, G.A.3
  • 27
    • 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., Fukuyama K. 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. 41:2002;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
  • 28
    • 0346003806 scopus 로고    scopus 로고
    • Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide: Implication for regiospecific hydroxylation of heme at the alpha-meso carbon
    • Sugishima M., Sakamoto H., Higashimoto Y., Omata Y., Hayashi S., Noguchi M., Fukuyama K. Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide: implication for regiospecific hydroxylation of heme at the alpha-meso carbon. J. Biol. Chem. 277:2002;45086-45090
    • (2002) J. Biol. Chem. , vol.277 , pp. 45086-45090
    • Sugishima, M.1    Sakamoto, H.2    Higashimoto, Y.3    Omata, Y.4    Hayashi, S.5    Noguchi, M.6    Fukuyama, K.7
  • 29
    • 0019590350 scopus 로고
    • Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: Involvement of hydroxyheme in the sequence of heme catabolism
    • Yoshida T., Noguchi M., Kikuchi G., Sano S. Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism. J. Biochem. (Tokyo). 90:1981;125-131
    • (1981) J. Biochem. (Tokyo) , vol.90 , pp. 125-131
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3    Sano, S.4
  • 30
    • 0017900548 scopus 로고
    • Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system
    • Yoshida T., Kikuchi G. Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system. J. Biol. Chem. 253:1978;4230-4236
    • (1978) J. Biol. Chem. , vol.253 , pp. 4230-4236
    • Yoshida, T.1    Kikuchi, G.2
  • 31
    • 0036494396 scopus 로고    scopus 로고
    • An open-flow cryostat using helium gas for cryogenic X-ray diffraction experiments
    • Nakasako M., Sawano M., Kawamoto M. An open-flow cryostat using helium gas for cryogenic X-ray diffraction experiments. Rev. Sci. Instrum. 73:2002;1318-1320
    • (2002) Rev. Sci. Instrum. , vol.73 , pp. 1318-1320
    • Nakasako, M.1    Sawano, M.2    Kawamoto, M.3
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 36
    • 0034503620 scopus 로고    scopus 로고
    • CONSCRIPT: A program for generating electron density isosurfaces for presentation in protein crystallography
    • Lawrence M.C., Bourke P. CONSCRIPT: a program for generating electron density isosurfaces for presentation in protein crystallography. J. Appl. Crystallog. 33:2000;990-991
    • (2000) J. Appl. Crystallog. , vol.33 , pp. 990-991
    • Lawrence, M.C.1    Bourke, P.2
  • 37
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt G.J., Jones T.A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallog. sect. D. 50:1994;178-185
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.