메뉴 건너뛰기




Volumn 117, Issue 15, 2013, Pages 4042-4049

Investigations of ferric heme cyanide photodissociation in myoglobin and horseradish peroxidase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHEMICAL REACTIONS; CYANIDES; PHOTOLYSIS; PORPHYRINS; TIME DOMAIN ANALYSIS;

EID: 84876466837     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp401224f     Document Type: Article
Times cited : (14)

References (45)
  • 1
    • 33847151331 scopus 로고    scopus 로고
    • --Vibrational Relaxation from Molecular Dynamics Simulations
    • --Vibrational Relaxation from Molecular Dynamics Simulations J. Phys. Chem. B 2007, 111, 218-226
    • (2007) J. Phys. Chem. B , vol.111 , pp. 218-226
    • Danielsson, J.1    Meuwly, M.2
  • 2
    • 0014429411 scopus 로고
    • The Electronic Structure of Protoheme Proteins. I. An Electron Paramagnetic Resonance and Optical Study of Horseradish Peroxidase and Its Derivatives
    • Blumberg, W. E.; Peisach, J.; Wittenberg, B. A.; Wittenberg, J. B. The Electronic Structure of Protoheme Proteins. I. An Electron Paramagnetic Resonance and Optical Study of Horseradish Peroxidase and Its Derivatives J. Biol. Chem. 1968, 243, 1854-1862
    • (1968) J. Biol. Chem. , vol.243 , pp. 1854-1862
    • Blumberg, W.E.1    Peisach, J.2    Wittenberg, B.A.3    Wittenberg, J.B.4
  • 3
    • 0014429446 scopus 로고
    • The Electronic Structure of Protoheme Proteins. II. An Electron Paramagnetic Resonance and Optical Study of Cytochrome C Peroxidase and Its Derivatives
    • Wittenberg, B. A.; Kampa, L.; Wittenberg, J. B.; Blumberg, W. E.; Peisach, J. The Electronic Structure of Protoheme Proteins. II. An Electron Paramagnetic Resonance and Optical Study of Cytochrome C Peroxidase and Its Derivatives J. Biol. Chem. 1968, 243, 1863-1870
    • (1968) J. Biol. Chem. , vol.243 , pp. 1863-1870
    • Wittenberg, B.A.1    Kampa, L.2    Wittenberg, J.B.3    Blumberg, W.E.4    Peisach, J.5
  • 4
    • 0014429488 scopus 로고
    • The Electronic Structure of Protoheme Proteins. III. Configuration of the Heme and Its Ligands
    • Peisach, J.; Blumberg, W. E.; Wittenberg, B. A.; Wittenberg, J. B. The Electronic Structure of Protoheme Proteins. III. Configuration of the Heme and Its Ligands J. Biol. Chem. 1968, 243, 1871-1880
    • (1968) J. Biol. Chem. , vol.243 , pp. 1871-1880
    • Peisach, J.1    Blumberg, W.E.2    Wittenberg, B.A.3    Wittenberg, J.B.4
  • 6
    • 0001052034 scopus 로고
    • Determination of the Orientation of the Magnetic Axes of the Cyano-Metmb Complexes of Point Mutants of Myoglobin by Solution 1h NMR: Influence of His E7 → Gly and Arg Cd3 → Gly Substitutions
    • Rajarathnam, K.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. Determination of the Orientation of the Magnetic Axes of the Cyano-Metmb Complexes of Point Mutants of Myoglobin by Solution 1h NMR: Influence of His E7 → Gly and Arg Cd3 → Gly Substitutions J. Am. Chem. Soc. 1992, 114, 9048-9058
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9048-9058
    • Rajarathnam, K.1    La Mar, G.N.2    Chiu, M.L.3    Sligar, S.G.4
  • 7
    • 0027245807 scopus 로고
    • Solution Structure Determination of the Heme Cavity in the E7 His → Val Cyano-Met Myoglobin Point Mutant Based on the Proton NMR Detected Dipolar Field of the Iron: Evidence for Contraction of the Heme Pocket
    • Rajarathnam, K.; Qin, J.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. Solution Structure Determination of the Heme Cavity in the E7 His → Val Cyano-Met Myoglobin Point Mutant Based on the Proton NMR Detected Dipolar Field of the Iron: Evidence for Contraction of the Heme Pocket Biochemistry 1993, 32, 5670-5680
    • (1993) Biochemistry , vol.32 , pp. 5670-5680
    • Rajarathnam, K.1    Qin, J.2    La Mar, G.N.3    Chiu, M.L.4    Sligar, S.G.5
  • 8
    • 0035844131 scopus 로고    scopus 로고
    • Solution 1h NMR of the Active Site of Substrate-Bound, Cyanide-Inhibited Human Heme Oxygenase: Comparison to the Crystal Structure of the Water-Ligated Form
    • La Mar, G. N.; Asokan, A.; Espiritu, B.; Yeh, D. C.; Auclair, K.; Ortiz de Montellano, P. R. Solution 1h NMR of the Active Site of Substrate-Bound, Cyanide-Inhibited Human Heme Oxygenase: Comparison to the Crystal Structure of the Water-Ligated Form J. Biol. Chem. 2001, 276, 15676-15687
    • (2001) J. Biol. Chem. , vol.276 , pp. 15676-15687
    • La Mar, G.N.1    Asokan, A.2    Espiritu, B.3    Yeh, D.C.4    Auclair, K.5    Ortiz De Montellano, P.R.6
  • 9
    • 0040924293 scopus 로고
    • Mössbauer Effect in Some Haemoglobin Compounds
    • Lang, G.; Marshali, W. Mössbauer Effect in Some Haemoglobin Compounds Proc. Phys. Soc. 1966, 87, 3-34
    • (1966) Proc. Phys. Soc. , vol.87 , pp. 3-34
    • Lang, G.1    Marshali, W.2
  • 10
    • 0032774244 scopus 로고    scopus 로고
    • Cyanide Binding to Lucina pectinata Hemoglobin i and to Sperm Whale Myoglobin: An X-ray Crystallographic Study
    • Bolognesi, M.; Rosano, C.; Losso, R.; Borassi, A.; Rizzi, M.; Wittenberg, J. B.; Boffi, A.; Ascenzi, P. Cyanide Binding to Lucina pectinata Hemoglobin I and to Sperm Whale Myoglobin: an X-ray Crystallographic Study Biophys. J. 1999, 77, 1093-1099
    • (1999) Biophys. J. , vol.77 , pp. 1093-1099
    • Bolognesi, M.1    Rosano, C.2    Losso, R.3    Borassi, A.4    Rizzi, M.5    Wittenberg, J.B.6    Boffi, A.7    Ascenzi, P.8
  • 12
    • 0021473156 scopus 로고
    • Iron-Carbon Bond Lengths in Carbonmonoxy and Cyanomet Complexes of the Monomeric Hemoglobin III from Chironomus Thummi Thummi: A Critical Comparison between Resonance Raman and X-Ray Diffraction Studies
    • Yu, N. T.; Benko, B.; Kerr, E. A.; Gersonde, K. Iron-Carbon Bond Lengths in Carbonmonoxy and Cyanomet Complexes of the Monomeric Hemoglobin III from Chironomus Thummi Thummi: A Critical Comparison between Resonance Raman and X-Ray Diffraction Studies Proc. Natl. Acad. Sci. U.S.A. 1984, 81, 5106-5110
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 5106-5110
    • Yu, N.T.1    Benko, B.2    Kerr, E.A.3    Gersonde, K.4
  • 13
    • 0022345516 scopus 로고
    • Spectroscopic Studies of Protein-Heme Interactions Accompanying the Allosteric Transition in Methemoglobins
    • Henry, E. R.; Rousseau, D. L.; Hopfield, J. J.; Noble, R. W.; Simon, S. R. Spectroscopic Studies of Protein-Heme Interactions Accompanying the Allosteric Transition in Methemoglobins Biochemistry 1985, 24, 5907-5918
    • (1985) Biochemistry , vol.24 , pp. 5907-5918
    • Henry, E.R.1    Rousseau, D.L.2    Hopfield, J.J.3    Noble, R.W.4    Simon, S.R.5
  • 15
    • 0025065381 scopus 로고
    • Metal-Ligand Vibrations of Cyanoferric Myeloperoxidase and Cyanoferric Horseradish Peroxidase: Evidence for a Constrained Heme Pocket in Myeloperoxidase
    • López-Garriga, J. J.; Oertling, W. A.; Kean, R. T.; Hoogland, H.; Wever, R.; Babcock, G. T. Metal-Ligand Vibrations of Cyanoferric Myeloperoxidase and Cyanoferric Horseradish Peroxidase: Evidence for a Constrained Heme Pocket in Myeloperoxidase Biochemistry 1990, 29, 9387-9395
    • (1990) Biochemistry , vol.29 , pp. 9387-9395
    • López-Garriga, J.J.1    Oertling, W.A.2    Kean, R.T.3    Hoogland, H.4    Wever, R.5    Babcock, G.T.6
  • 16
    • 0027501847 scopus 로고
    • Distinct Heme Active-Site Structure in Lactoperoxidase Revealed by Resonance Raman Spectroscopy
    • Hu, S.; Treat, R. W.; Kincaid, J. R. Distinct Heme Active-Site Structure in Lactoperoxidase Revealed by Resonance Raman Spectroscopy Biochemistry 1993, 32, 10125-10130
    • (1993) Biochemistry , vol.32 , pp. 10125-10130
    • Hu, S.1    Treat, R.W.2    Kincaid, J.R.3
  • 17
    • 0028279008 scopus 로고
    • Resonance Raman Study of Cyanide-Ligated Horseradish Peroxidase. Detection of Two Binding Geometries and Direct Evidence for the "push-Pull" Effect
    • Al-Mustafa, J.; Kincaid, J. R. Resonance Raman Study of Cyanide-Ligated Horseradish Peroxidase. Detection of Two Binding Geometries and Direct Evidence for the "Push-Pull" Effect Biochemistry 1994, 33, 2191-2197
    • (1994) Biochemistry , vol.33 , pp. 2191-2197
    • Al-Mustafa, J.1    Kincaid, J.R.2
  • 18
    • 0000301740 scopus 로고
    • Resonance Raman Spectroscopic Detection of Both Linear and Bent Fe-CN Fragments for the Cyanide Adducts of Cytochrome P-450 Camphor and Its Substrate-Bound Forms. Relevance to the "charge Relay" Mechanism
    • Simianu, M. C.; Kincaid, J. R. Resonance Raman Spectroscopic Detection of Both Linear and Bent Fe-CN Fragments for the Cyanide Adducts of Cytochrome P-450 Camphor and Its Substrate-Bound Forms. Relevance to the "Charge Relay" Mechanism J. Am. Chem. Soc. 1995, 117, 4628-4636
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 4628-4636
    • Simianu, M.C.1    Kincaid, J.R.2
  • 19
    • 1842513886 scopus 로고    scopus 로고
    • - Adducts of Hemoglobin, Myoglobin, and Cytochrome C Oxidase: Evidence for Vibrational Coupling between the Fe-C-N Bending and Porphyrin in-Plane Modes
    • - Adducts of Hemoglobin, Myoglobin, and Cytochrome C Oxidase: Evidence for Vibrational Coupling between the Fe-C-N Bending and Porphyrin in-Plane Modes J. Phys. Chem. 1996, 100, 15274-15279
    • (1996) J. Phys. Chem. , vol.100 , pp. 15274-15279
    • Hirota, S.1    Ogura, T.2    Shinzawaitoh, K.3    Yoshikawa, S.4    Kitagawa, T.5
  • 20
    • 0034322841 scopus 로고    scopus 로고
    • Distal Interactions in the Cyanide Complex of Ferric Chlamydomonas Hemoglobin
    • Das, T. K.; Couture, M.; Guertin, M.; Rousseau, D. L. Distal Interactions in the Cyanide Complex of Ferric Chlamydomonas Hemoglobin J. Phys. Chem. B 2000, 104, 10750-10756
    • (2000) J. Phys. Chem. B , vol.104 , pp. 10750-10756
    • Das, T.K.1    Couture, M.2    Guertin, M.3    Rousseau, D.L.4
  • 23
    • 42149133790 scopus 로고    scopus 로고
    • Investigations of Vibrational Coherence in the Low-Frequency Region of Ferric Heme Proteins
    • Gruia, F.; Kubo, M.; Ye, X.; Champion, P. M. Investigations of Vibrational Coherence in the Low-Frequency Region of Ferric Heme Proteins Biophys. J. 2008, 94, 2252-2268
    • (2008) Biophys. J. , vol.94 , pp. 2252-2268
    • Gruia, F.1    Kubo, M.2    Ye, X.3    Champion, P.M.4
  • 24
    • 84875485525 scopus 로고    scopus 로고
    • Ultrafast Tryptophan-to-Heme Electron Transfer in Myoglobins Revealed by UV 2D Spectroscopy
    • 10.1126/science.1230758
    • Consani, C.; Auböck, G.; van Mourik, F.; Chergui, M. Ultrafast Tryptophan-to-Heme Electron Transfer in Myoglobins Revealed by UV 2D Spectroscopy Science 2013, 10.1126/science.1230758
    • (2013) Science
    • Consani, C.1    Auböck, G.2    Van Mourik, F.3    Chergui, M.4
  • 25
    • 0021989717 scopus 로고
    • Investigations of Cyanide as an Infrared Probe of Hemeprotein Ligand Binding Sites
    • Yoshikawa, S.; O'Keeffe, D. H.; Caughey, W. S. Investigations of Cyanide as an Infrared Probe of Hemeprotein Ligand Binding Sites J. Biol. Chem. 1985, 260, 3518-3528
    • (1985) J. Biol. Chem. , vol.260 , pp. 3518-3528
    • Yoshikawa, S.1    O'Keeffe, D.H.2    Caughey, W.S.3
  • 28
    • 0001340863 scopus 로고
    • Kinetische Untersuchungen über die Bildung von Metmyoglobin- komplexen
    • Blanck, J.; Graf, W.; Scheler, U. W. Kinetische Untersuchungen über die Bildung von Metmyoglobin-komplexen Acta Biol. Med. Ger. 1961, 7, 323-326
    • (1961) Acta Biol. Med. Ger. , vol.7 , pp. 323-326
    • Blanck, J.1    Graf, W.2    Scheler, U.W.3
  • 29
    • 84986793530 scopus 로고
    • Resonance Raman Spectroscopy of Heme Proteins with Intensified Vidicon Detectors: Studies of Low Frequency Modes and Excitation Profiles in Cytochrome c and Hemoglobin
    • Yu, N.-T.; Srivastava, R. B. Resonance Raman Spectroscopy of Heme Proteins with Intensified Vidicon Detectors: Studies of Low Frequency Modes and Excitation Profiles in Cytochrome c and Hemoglobin J. Raman Spectrosc. 1980, 9, 166-171
    • (1980) J. Raman Spectrosc. , vol.9 , pp. 166-171
    • Yu, N.-T.1    Srivastava, R.B.2
  • 32
    • 0014301290 scopus 로고
    • The Kinetics of Cyanide and Fluoride Binding by Ferric Horseradish Peroxidase
    • Ellis, W. D.; Dunford, H. B. The Kinetics of Cyanide and Fluoride Binding by Ferric Horseradish Peroxidase Biochemistry 1968, 7, 2054-2062
    • (1968) Biochemistry , vol.7 , pp. 2054-2062
    • Ellis, W.D.1    Dunford, H.B.2
  • 35
    • 0025697456 scopus 로고
    • Picosecond Flash Photolysis of Carboxy Horseradish Peroxidase: Rapid Geminate Recombination in the Presence of Benzohydroxamic Acid
    • Berinstain, A. B.; English, A. M.; Hill, B. C.; Sharma, D. Picosecond Flash Photolysis of Carboxy Horseradish Peroxidase: Rapid Geminate Recombination in the Presence of Benzohydroxamic Acid J. Am. Chem. Soc. 1990, 112, 9649-9651
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9649-9651
    • Berinstain, A.B.1    English, A.M.2    Hill, B.C.3    Sharma, D.4
  • 37
    • 0023660146 scopus 로고
    • Recombination of Carbon Monoxide to Ferrous Horseradish Peroxidase Types A and C
    • Doster, W.; Bowne, S. F.; Frauenfelder, H.; Reinisch, L.; Shyamsunder, E. Recombination of Carbon Monoxide to Ferrous Horseradish Peroxidase Types A and C J. Mol. Biol. 1987, 194, 299-312
    • (1987) J. Mol. Biol. , vol.194 , pp. 299-312
    • Doster, W.1    Bowne, S.F.2    Frauenfelder, H.3    Reinisch, L.4    Shyamsunder, E.5
  • 38
    • 0022973920 scopus 로고
    • PH Dependence of Carbon Monoxide Binding to Ferrous Horseradish Peroxidase
    • Coletta, M. A., F.; Brunori, M.; Traylor, T. G. pH Dependence of Carbon Monoxide Binding to Ferrous Horseradish Peroxidase J. Biol. Chem. 1986, 261, 9811-9814
    • (1986) J. Biol. Chem. , vol.261 , pp. 9811-9814
    • Coletta, M.A..F.1    Brunori, M.2    Traylor, T.G.3
  • 39
    • 32244442436 scopus 로고    scopus 로고
    • Dynamics of Nitric Oxide Rebinding and Escape in Horseradish Peroxidase
    • Ye, X.; Yu, A.; Champion, P. M. Dynamics of Nitric Oxide Rebinding and Escape in Horseradish Peroxidase J. Am. Chem. Soc. 2006, 128, 1444-1445
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1444-1445
    • Ye, X.1    Yu, A.2    Champion, P.M.3
  • 40
    • 0027453672 scopus 로고
    • Investigations of Ligand Association and Dissociation Rates in the "open" and "closed" States of Myoglobin
    • Tian, W. D.; Sage, J. T.; Champion, P. M. Investigations of Ligand Association and Dissociation Rates in the "Open" and "Closed" States of Myoglobin J. Mol. Biol. 1993, 233, 155-166
    • (1993) J. Mol. Biol. , vol.233 , pp. 155-166
    • Tian, W.D.1    Sage, J.T.2    Champion, P.M.3
  • 41
    • 0000379278 scopus 로고    scopus 로고
    • Probing Heme Protein Conformational Equilibration Rates with Kinetic Selection
    • Tian, W. D.; Sage, J. T.; Champion, P. M.; Chien, E.; Sligar, S. G. Probing Heme Protein Conformational Equilibration Rates with Kinetic Selection Biochemistry 1996, 35, 3487-3502
    • (1996) Biochemistry , vol.35 , pp. 3487-3502
    • Tian, W.D.1    Sage, J.T.2    Champion, P.M.3    Chien, E.4    Sligar, S.G.5
  • 42
    • 0014030651 scopus 로고
    • An X-ray Study of Azide Methaemoglobin
    • Perutz, M. F.; Mathews, F. S. An X-ray Study of Azide Methaemoglobin J. Mol. Biol. 1966, 21, 199-202
    • (1966) J. Mol. Biol. , vol.21 , pp. 199-202
    • Perutz, M.F.1    Mathews, F.S.2
  • 43
    • 0018791973 scopus 로고
    • Dynamics of Ligand Binding to Heme Proteins
    • Case, D. A.; Karplus, M. Dynamics of Ligand Binding to Heme Proteins J. Mol. Biol. 1979, 132, 343-368
    • (1979) J. Mol. Biol. , vol.132 , pp. 343-368
    • Case, D.A.1    Karplus, M.2
  • 45
    • 0024334934 scopus 로고
    • Resonance Raman Investigations of Site-Directed Mutants of Myoglobin: Effects of Distal Histidine Replacement
    • Morikis, D.; Champion, P. M.; Springer, B. A.; Sligar, S. G. Resonance Raman Investigations of Site-Directed Mutants of Myoglobin: Effects of Distal Histidine Replacement Biochemistry 1989, 28, 4791-4800
    • (1989) Biochemistry , vol.28 , pp. 4791-4800
    • Morikis, D.1    Champion, P.M.2    Springer, B.A.3    Sligar, S.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.