메뉴 건너뛰기




Volumn 26, Issue 5, 2013, Pages 839-852

Erratum: Conversion of a heme-based oxygen sensor to a heme oxygenase by hydrogen sulfide: Effects of mutations in the heme distal side of a heme-based oxygen sensor phosphodiesterase (Ec DOS)(biometals, (2013) 26, (839-852), 10.1007/s10534-013-9640-4);Conversion of a heme-based oxygen sensor to a heme oxygenase by hydrogen sulfide: Effects of mutations in the heme distal side of a heme-based oxygen sensor phosphodiesterase (Ec DOS)

Author keywords

Heme oxygenase; Heme protein; Hydrogen sulphide; Oxygen sensor; Reactive oxygen species; Verdoheme

Indexed keywords

FERRIC ION; HEME; HEME OXYGENASE; HYDROGEN PEROXIDE; HYDROGEN SULFIDE; OXYGEN; PHOSPHODIESTERASE; REACTIVE OXYGEN METABOLITE;

EID: 85027929178     PISSN: 09660844     EISSN: 15728773     Source Type: Journal    
DOI: 10.1007/s10534-013-9662-y     Document Type: Erratum
Times cited : (11)

References (42)
  • 1
    • 0021734882 scopus 로고
    • Sulfmyoglobin. Resonance Raman spectroscopic evidence for an iron-chlorin prosthetic group
    • Andersson LA, Loehr TM, Lim AR, Mauk AG (1984) Sulfmyoglobin. Resonance Raman spectroscopic evidence for an iron-chlorin prosthetic group. J Biol Chem 259:15340–15349.
    • (1984) J Biol Chem , vol.259 , pp. 15340-15349
    • Andersson, L.A.1    Loehr, T.M.2    Lim, A.R.3    Mauk, A.G.4
  • 2
    • 10444248807 scopus 로고    scopus 로고
    • The sulfide binding function of annelid hemoglobins: Relic of an old biosystem?
    • Bailly X, Vinogradov S (2005) The sulfide binding function of annelid hemoglobins: relic of an old biosystem? J Inorg Biochem 99:142–150.
    • (2005) J Inorg Biochem , vol.99 , pp. 142-150
    • Bailly, X.1    Vinogradov, S.2
  • 3
    • 85045959738 scopus 로고    scopus 로고
    • Hydrogen sulfide: Redox metabolism and signaling
    • Banerjee R (2012) Hydrogen sulfide: redox metabolism and signaling. Antioxid Redox Signal 17:45–57.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 45-57
    • Banerjee, R.1
  • 4
    • 0015239532 scopus 로고
    • Sulfheme proteins. I. Optical and magnetic properties of sulfmyoglobin and its derivatives
    • Berzofsky JA, Peisach J, Blumber WE (1971a) Sulfheme proteins. I. Optical and magnetic properties of sulfmyoglobin and its derivatives. J Biol Chem 246:3367–3377.
    • (1971) J Biol Chem , vol.246 , pp. 3367-3377
    • Berzofsky, J.A.1    Peisach, J.2    Blumber, W.E.3
  • 5
    • 0015219041 scopus 로고
    • Sulfheme proteins. II. The reversible oxygenation of ferrous sulfmyoglobin
    • Berzofsky JA, Peisach J, Blumberg WE (1971b) Sulfheme proteins. II. The reversible oxygenation of ferrous sulfmyoglobin. J Biol Chem 246:7366–7372.
    • (1971) J Biol Chem , vol.246 , pp. 7366-7372
    • Berzofsky, J.A.1    Peisach, J.2    Blumberg, W.E.3
  • 7
    • 0018786581 scopus 로고
    • Oxidation of horseradish peroxidase compound II to compound I
    • Hewson WD, Hager LP (1979) Oxidation of horseradish peroxidase compound II to compound I. J Biol Chem 254:3182–3186.
    • (1979) J Biol Chem , vol.254 , pp. 3182-3186
    • Hewson, W.D.1    Hager, L.P.2
  • 8
    • 0344393534 scopus 로고    scopus 로고
    • Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli: Optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials
    • Hirata S, Matsui T, Sasakura Y, Sugiyama S, Yoshimura T, Sagami I, Shimizu T (2003) Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli: optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials. Eur J Biochem 270:4771–4779.
    • (2003) Eur J Biochem , vol.270 , pp. 4771-4779
    • Hirata, S.1    Matsui, T.2    Sasakura, Y.3    Sugiyama, S.4    Yoshimura, T.5    Sagami, I.6    Shimizu, T.7
  • 9
    • 80053920510 scopus 로고    scopus 로고
    • Emerging role of heme as a signal and the gas-sensing site: Heme-sensing and gas-sensing proteins
    • Kadish KM, Smith KM, Guilard R, World Scientific Hackensack, USA
    • Igarashi J, Kitanishi K, Shimizu T (2011) Emerging role of heme as a signal and the gas-sensing site: heme-sensing and gas-sensing proteins. In: Kadish KM, Smith KM, Guilard R (eds) Handbook of porphyrin science, vol 15. World Scientific Hackensack, USA, pp 399–460.
    • (2011) Handbook of Porphyrin Science , vol.15 , pp. 399-460
    • Igarashi, J.1    Kitanishi, K.2    Shimizu, T.3
  • 11
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • Kabil O, Banerjee R (2010) Redox biochemistry of hydrogen sulfide. J Biol Chem 285:21903–21907.
    • (2010) J Biol Chem , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 12
    • 84860761445 scopus 로고    scopus 로고
    • Hydrogen sulfide is a signaling molecule and a cytoprotectant
    • Kimura H, Shibuya N, Kimura Y (2012) Hydrogen sulfide is a signaling molecule and a cytoprotectant. Antioxid Redox Signal 17:45–57.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 45-57
    • Kimura, H.1    Shibuya, N.2    Kimura, Y.3
  • 14
    • 80053896156 scopus 로고    scopus 로고
    • Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5
    • Kitanishi K, Kobayashi K, Uchida T, Ishimori K, Igarashi J, Shimizu T (2011) Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5. J Biol Chem 286:35522–35534.
    • (2011) J Biol Chem , vol.286 , pp. 35522-35534
    • Kitanishi, K.1    Kobayashi, K.2    Uchida, T.3    Ishimori, K.4    Igarashi, J.5    Shimizu, T.6
  • 15
    • 0025026382 scopus 로고
    • Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands
    • Kraus DW, Wittenberg JB (1990) Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands. J Biol Chem 265:16043–16053.
    • (1990) J Biol Chem , vol.265 , pp. 16043-16053
    • Kraus, D.W.1    Wittenberg, J.B.2
  • 16
    • 0025167226 scopus 로고
    • Hemoglobins of the Lucina pectinata/bateria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins
    • Kraus DW, Wittenberg JB, Jin-Fen L, Peisach J (1990) Hemoglobins of the Lucina pectinata/bateria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins. J Biol Chem 265:16054–16059.
    • (1990) J Biol Chem , vol.265 , pp. 16054-16059
    • Kraus, D.W.1    Wittenberg, J.B.2    Jin-Fen, L.3    Peisach, J.4
  • 17
    • 2442624510 scopus 로고    scopus 로고
    • A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor
    • Kurokawa H, Lee DS, Watanabe M, Sagami I, Mikami B, Raman CS, Shimizu T (2004) A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor. J Biol Chem 279:20186–20193.
    • (2004) J Biol Chem , vol.279 , pp. 20186-20193
    • Kurokawa, H.1    Lee, D.S.2    Watanabe, M.3    Sagami, I.4    Mikami, B.5    Raman, C.S.6    Shimizu, T.7
  • 18
    • 0028208553 scopus 로고
    • Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli
    • Lloyd E, Mauk AG (1994) Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli. FEBS Lett 340:281–286.
    • (1994) FEBS Lett , vol.340 , pp. 281-286
    • Lloyd, E.1    Mauk, A.G.2
  • 19
    • 0031468071 scopus 로고    scopus 로고
    • On the formation and reactivity of compound I of the His-64 myoglobin mutants
    • Matsui T, Ozaki S, Watanabe Y (1997) On the formation and reactivity of compound I of the His-64 myoglobin mutants. J Biol Chem 272:32735–32738.
    • (1997) J Biol Chem , vol.272 , pp. 32735-32738
    • Matsui, T.1    Ozaki, S.2    Watanabe, Y.3
  • 20
    • 77950992025 scopus 로고    scopus 로고
    • Dioxygen activation for the self-degradation of heme: Reaction mechanism and regulation of heme oxygenase
    • Matsui T, Iwasaki M, Sugiyama R, Unno M, Ikeda-Saito M (2010) Dioxygen activation for the 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
  • 22
    • 0542422859 scopus 로고    scopus 로고
    • Heme oxygenase mechanistic evidence for an electrophilic ferric peroxide species
    • Ortiz de Montellano PR (1998) Heme oxygenase mechanistic 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
  • 23
    • 1542327658 scopus 로고    scopus 로고
    • Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli DOS heme domain (Ec DOSH)
    • Park H, Suquet C, Satterlee JD, Kang C (2004) Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli DOS heme domain (Ec DOSH). Biochemistry 43:2738–2746.
    • (2004) Biochemistry , vol.43 , pp. 2738-2746
    • Park, H.1    Suquet, C.2    Satterlee, J.D.3    Kang, C.4
  • 24
    • 84864285556 scopus 로고    scopus 로고
    • 2S signalling through protein sulfhydration and beyond
    • 2S signalling 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
  • 27
    • 79951882093 scopus 로고    scopus 로고
    • Thiol/disulfide redox switches in the regulation of heme binding to proteins
    • Ragsdale SW, Yi L (2011) Thiol/disulfide redox switches in the regulation of heme binding to proteins. Antioxid Redox Signal 14:1039–1047.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 1039-1047
    • Ragsdale, S.W.1    Yi, L.2
  • 29
    • 0033733182 scopus 로고    scopus 로고
    • Separation and identification of regioisomers of verdoheme by reverse-phase ion-pair high-performance liquid chromatography, and characterization of their complexes with heme oxygenase
    • Sakamoto H, Omata Y, Adachi Y, Palmer G, Noguchi M (2000) Separation and identification of regioisomers of verdoheme by reverse-phase ion-pair high-performance liquid chromatography, and characterization of their complexes with heme oxygenase. J Inorg Biochem 82:113–121.
    • (2000) J Inorg Biochem , vol.82 , pp. 113-121
    • Sakamoto, H.1    Omata, Y.2    Adachi, Y.3    Palmer, G.4    Noguchi, M.5
  • 30
    • 33344477903 scopus 로고    scopus 로고
    • Structure-function relationships of EcDOS, a hemeregulated phosphodiesterase from Escherichia coli
    • Sasakura Y, Yoshimura-Suzuki T, Kurokawa H, Shimizu T (2006) Structure-function relationships of EcDOS, a hemeregulated phosphodiesterase from Escherichia coli. Acc Chem Res 39:37–43.
    • (2006) Acc Chem Res , vol.39 , pp. 37-43
    • Sasakura, Y.1    Yoshimura-Suzuki, T.2    Kurokawa, H.3    Shimizu, T.4
  • 31
    • 0001023291 scopus 로고    scopus 로고
    • The molecular mechanism of autooxidation for myoglobin and hemoglobin: A venerable puzzle
    • Shikama K (1998) The molecular mechanism of autooxidation for myoglobin and hemoglobin: a venerable puzzle. Chem Rev 98:1357–1374.
    • (1998) Chem Rev , vol.98 , pp. 1357-1374
    • Shikama, K.1
  • 32
    • 84858449270 scopus 로고    scopus 로고
    • Binding of cysteine thiolate to the Fe(III) heme complex is critical for the function of heme sensor proteins
    • Shimizu T (2012) Binding of cysteine thiolate to the Fe(III) heme complex is critical for the function of heme sensor proteins. J Inorg Biochem 108:171–177.
    • (2012) J Inorg Biochem , vol.108 , pp. 171-177
    • Shimizu, T.1
  • 34
    • 84868138296 scopus 로고    scopus 로고
    • 2 in heme oxygenase: Comparison of static structures and dynamic conformation changes following CO photolysis
    • 2 in heme oxygenase: comparison of static structures and dynamic conformation changes following CO photolysis. Biochemistry 51:8554–8562.
    • (2012) Biochemistry , vol.51 , pp. 8554-8562
    • Sugishima, M.1    Moffat, K.2    Noguchi, M.3
  • 35
    • 35748959038 scopus 로고    scopus 로고
    • Hydrogen sulphide and its therapeutic potential
    • Szabo C (2007) Hydrogen sulphide and its therapeutic potential. Nature Rev Drug Disco 6:917–935.
    • (2007) Nature Rev Drug Disco , vol.6 , pp. 917-935
    • Szabo, C.1
  • 36
    • 78649439251 scopus 로고    scopus 로고
    • Gaseotransmitters: New frontiers for translational science
    • Szabo C (2010) Gaseotransmitters: new frontiers for translational science. Sci Transl Med 2(59):ps54.
    • (2010) Sci Transl Med , vol.2 , Issue.59
    • Szabo, C.1
  • 37
    • 0942276394 scopus 로고    scopus 로고
    • Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli: Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met95 mutants
    • Taguchi S, Matsui T, Igarashi J, Sasakura Y, Araki Y, Ito O, Sugiyama S, Sagami I, Shimizu T (2004) Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli: kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met95 mutants. J Biol Chem 279:3340–3347.
    • (2004) J Biol Chem , vol.279 , pp. 3340-3347
    • Taguchi, S.1    Matsui, T.2    Igarashi, J.3    Sasakura, Y.4    Araki, Y.5    Ito, O.6    Sugiyama, S.7    Sagami, I.8    Shimizu, T.9
  • 38
    • 84862809750 scopus 로고    scopus 로고
    • Hydrogen sulfide stimulates the catalytic activity of a heme-regulated phosphodiesterase from Escherichia coli (Ec DOS)
    • Takahashi H, Sekimoto M, Tanaka M, Tanaka A, Igarashi J, Shimizu T (2012) Hydrogen sulfide stimulates the catalytic activity of a heme-regulated phosphodiesterase from Escherichia coli (Ec DOS). J Inorg Biochem 109:66–71.
    • (2012) J Inorg Biochem , vol.109 , pp. 66-71
    • Takahashi, H.1    Sekimoto, M.2    Tanaka, M.3    Tanaka, A.4    Igarashi, J.5    Shimizu, T.6
  • 39
    • 57649114078 scopus 로고    scopus 로고
    • Ligand binding to the Fe(III)- protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: Roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand binding
    • Tanaka A, Shimizu T (2008) Ligand binding to the Fe(III)- protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand binding. Biochemistry 47:13438–13446.
    • (2008) Biochemistry , vol.47 , pp. 13438-13446
    • Tanaka, A.1    Shimizu, T.2
  • 40
    • 34547137430 scopus 로고    scopus 로고
    • Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP
    • Tanaka A, Takahashi H, Shimizu T (2007) Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP. J Biol Chem 282:21301–21307.
    • (2007) J Biol Chem , vol.282 , pp. 21301-21307
    • Tanaka, A.1    Takahashi, H.2    Shimizu, T.3
  • 41
    • 77950805698 scopus 로고    scopus 로고
    • Hydrogen sulfide: The third gaseotransmitter in biology andmedicine
    • Wang R (2010) Hydrogen sulfide: the third gaseotransmitter in biology andmedicine. Antioxid Redox Signal 12:1061–1064.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 1061-1064
    • Wang, R.1
  • 42
    • 0036436657 scopus 로고    scopus 로고
    • Unusual cyanide bindings to a heme-regulated phosphodiesterase from Escherichia coli: Effect of Met95 mutations
    • Watanabe M, Matsui T, Sasakura Y, Sagami I, Shimizu T (2002) Unusual cyanide bindings to a heme-regulated phosphodiesterase from Escherichia coli: effect of Met95 mutations. Biochem Biophys Res Commun 299:169–172
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 169-172
    • Watanabe, M.1    Matsui, T.2    Sasakura, Y.3    Sagami, I.4    Shimizu, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.