메뉴 건너뛰기




Volumn 77, Issue 2, 1999, Pages 1143-1149

Pentacoordinate hemin derivatives in sodium dodecyl sulfate micelles: Model systems for the assignment of the fifth ligand in ferric heme proteins

Author keywords

[No Author keywords available]

Indexed keywords

DODECYL SULFATE SODIUM; HEMIN; HEMOPROTEIN; IRON; WATER;

EID: 0032815529     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76965-1     Document Type: Article
Times cited : (96)

References (31)
  • 1
    • 0001098626 scopus 로고
    • 15N substituted derivatives. II. A normal coordinate analysis
    • 15N substituted derivatives. II. A normal coordinate analysis. J. Chem. Phys. 69: 4526-4534.
    • (1978) J. Chem. Phys. , vol.69 , pp. 4526-4534
    • Abe, M.1    Kitagawa, T.2    Kyogoku, T.3
  • 3
    • 0018802936 scopus 로고
    • Resonance Raman examination of axial ligand bonding and spin-state equilibria in metmyoglobin hydroxide and other heme derivatives
    • Asher, S. A., and T. M. Schuster. 1979. Resonance Raman examination of axial ligand bonding and spin-state equilibria in metmyoglobin hydroxide and other heme derivatives. Biochemistry. 18:5377-5387.
    • (1979) Biochemistry , vol.18 , pp. 5377-5387
    • Asher, S.A.1    Schuster, T.M.2
  • 4
    • 0000990636 scopus 로고    scopus 로고
    • Cyanide binding to phthalocyaninato iron (II) in dimethyl sulfoxide in the presence of carbon monoxide: Kinetic and equilibrium study
    • Boffi, A., C. Ercolani, F. Monacelli, and P. Ascenzi. 1998. Cyanide binding to phthalocyaninato iron (II) in dimethyl sulfoxide in the presence of carbon monoxide: kinetic and equilibrium study. Inorg. Chim. Acta. 267:109-114.
    • (1998) Inorg. Chim. Acta , vol.267 , pp. 109-114
    • Boffi, A.1    Ercolani, C.2    Monacelli, F.3    Ascenzi, P.4
  • 5
    • 0028096564 scopus 로고
    • Structural characterization of oxidized dimeric Scapharca inaequivalvis hemoglobin by resonance Raman spectroscopy
    • Boffi, A., S. Takahashi, C. Spagnuolo, D. L. Rousseau, and E. Chiancone. 1994. Structural characterization of oxidized dimeric Scapharca inaequivalvis hemoglobin by resonance Raman spectroscopy. J. Biol. Chem. 269:20437-20440.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20437-20440
    • Boffi, A.1    Takahashi, S.2    Spagnuolo, C.3    Rousseau, D.L.4    Chiancone, E.5
  • 6
    • 0029089642 scopus 로고
    • Origin of the pH-dependent spectroscopic properties of pentacoordinate metmyoglobin variants
    • Bogumil, R., R. Maurus, D. P. Hildebrand, G. D. Brayer, and A. G. Mauk. 1995. Origin of the pH-dependent spectroscopic properties of pentacoordinate metmyoglobin variants. Biochemistry. 34:10483-10490.
    • (1995) Biochemistry , vol.34 , pp. 10483-10490
    • Bogumil, R.1    Maurus, R.2    Hildebrand, D.P.3    Brayer, G.D.4    Mauk, A.G.5
  • 7
    • 0033613930 scopus 로고    scopus 로고
    • Hydroxide rather than histidine is coordinated to the heme in five-coordinate ferric Scapharca inaequivalvis hemoglobin
    • Das, T. K., A. Boffi, E. Chiancone, and D. L. Rousseau. 1999a. Hydroxide rather than histidine is coordinated to the heme in five-coordinate ferric Scapharca inaequivalvis hemoglobin. J. Biol. Chem. 274:2916-2919.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2916-2919
    • Das, T.K.1    Boffi, A.2    Chiancone, E.3    Rousseau, D.L.4
  • 10
    • 28444477603 scopus 로고
    • K. Smith, editor. Elsevier Scientific Publishing Co., Amsterdam, the Netherlands.
    • Falk, J. E. 1975. In Porphyrins and Metalloporphyrins. K. Smith, editor. Elsevier Scientific Publishing Co., Amsterdam, the Netherlands. 805-807.
    • (1975) Porphyrins and Metalloporphyrins , pp. 805-807
    • Falk, J.E.1
  • 11
    • 0028354425 scopus 로고
    • Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin and horseradish peroxidase at room and low temperatures
    • Feis, A., M. P. Marzocchi, M. Paoli, and G. Smulevich. 1994. Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin and horseradish peroxidase at room and low temperatures. Biochemistry. 33:4577-4583.
    • (1994) Biochemistry , vol.33 , pp. 4577-4583
    • Feis, A.1    Marzocchi, M.P.2    Paoli, M.3    Smulevich, G.4
  • 13
    • 33847085258 scopus 로고
    • Iron-ligand stretching band in the resonance Raman spectra of ferrous iron porphyrin derivatives. Importance as a probe band for quaternary structure of hemoglobin
    • Hori, H., and T. Kitagawa. 1980. Iron-ligand stretching band in the resonance Raman spectra of ferrous iron porphyrin derivatives. Importance as a probe band for quaternary structure of hemoglobin. J. Am. Chem. Soc. 102:3608-3613.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 3608-3613
    • Hori, H.1    Kitagawa, T.2
  • 14
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin
    • Hu, S., K. M. Smith, and T. G. Spiro. 1996. Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118:12638-12646.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12638-12646
    • Hu, S.1    Smith, K.M.2    Spiro, T.G.3
  • 15
    • 0039667195 scopus 로고
    • Use of one electron theory for the interpretation of near edge structure in K-shell x-ray absorption spectra of transition metal complexes
    • Kutzler, F. W., C. R. Natoli, D. K. Misemer, S. Doniach, and K. O. Hogdson. 1980. Use of one electron theory for the interpretation of near edge structure in K-shell x-ray absorption spectra of transition metal complexes. J. Chem. Phys. 73:3274-3288.
    • (1980) J. Chem. Phys. , vol.73 , pp. 3274-3288
    • Kutzler, F.W.1    Natoli, C.R.2    Misemer, D.K.3    Doniach, S.4    Hogdson, K.O.5
  • 17
    • 33751156464 scopus 로고
    • Dynamics of porphyrin molecules in micelles. Picosecond time-resolved fluorescence anisotropy studies. 7
    • Maiti, N. C., S. Mazumdar, and N. Periasamy. 1995. Dynamics of porphyrin molecules in micelles. Picosecond time-resolved fluorescence anisotropy studies. 7. Phys. Chem. 99:10708-10715.
    • (1995) Phys. Chem. , vol.99 , pp. 10708-10715
    • Maiti, N.C.1    Mazumdar, S.2    Periasamy, N.3
  • 18
    • 0017198224 scopus 로고
    • Visible absorption spectra of quantum mixed-spin ferric heme proteins
    • Maltempo, M. M. 1976. Visible absorption spectra of quantum mixed-spin ferric heme proteins. Biochim. Biophys. Acta. 434:513-518.
    • (1976) Biochim. Biophys. Acta , vol.434 , pp. 513-518
    • Maltempo, M.M.1
  • 19
    • 0000805673 scopus 로고
    • Biomimetic chemistry of hemes inside aqueous micelles
    • Mazumdar, S., and S. Mitra. 1993. Biomimetic chemistry of hemes inside aqueous micelles. Structure Bonding. 81:115-145.
    • (1993) Structure Bonding , vol.81 , pp. 115-145
    • Mazumdar, S.1    Mitra, S.2
  • 20
    • 0025330643 scopus 로고
    • Resonance Raman studies of iron spin and axial coordination in distal pocket mutants of ferric myoglobin. 7
    • Morikis, D., P. M. Champion, B. A. Springer, K. A. Egeberg, and S. G. Sligar. 1990. Resonance Raman studies of iron spin and axial coordination in distal pocket mutants of ferric myoglobin. 7. Biol. Chem. 265:12143-12145.
    • (1990) Biol. Chem. , vol.265 , pp. 12143-12145
    • Morikis, D.1    Champion, P.M.2    Springer, B.A.3    Egeberg, K.A.4    Sligar, S.G.5
  • 22
    • 0000472143 scopus 로고
    • Iron-hydroxide stretching resonance Raman bands of a water-soluble sterically hindered porphyrin
    • Reed, R. A., K. R. Rodgers, K. Kushmeider, T. G. Spiro, and Y. O. Su. 1990. Iron-hydroxide stretching resonance Raman bands of a water-soluble sterically hindered porphyrin. Inorg. Chem. 29:2881-2883.
    • (1990) Inorg. Chem. , vol.29 , pp. 2881-2883
    • Reed, R.A.1    Rodgers, K.R.2    Kushmeider, K.3    Spiro, T.G.4    Su, Y.O.5
  • 23
    • 0003097351 scopus 로고
    • Raman difference spectroscopy as a probe of biological molecule
    • Rousseau, D. L. 1981. Raman difference spectroscopy as a probe of biological molecule. J. Raman Spectrosc. 10:94-99.
    • (1981) J. Raman Spectrosc. , vol.10 , pp. 94-99
    • Rousseau, D.L.1
  • 25
    • 33751390964 scopus 로고
    • Xanes spectra of copper II complexes: Correlation of the intensity of the 1s-3d transition
    • Sano, M., S. Komorita, and H. Yamatera. 1992. Xanes spectra of copper II complexes: correlation of the intensity of the 1s-3d transition. Inorg. Chem. 31:459-463.
    • (1992) Inorg. Chem. , vol.31 , pp. 459-463
    • Sano, M.1    Komorita, S.2    Yamatera, H.3
  • 26
    • 0025090930 scopus 로고
    • X-ray absorption spectral study of ferric high spin hemeproteins: XANES evidence for coordination structure of the heme iron
    • Shiro, Y., F. Sato, T. Suzuki, T. Izuka, T. Matsushita, and H. Oyanagi. 1990. X-ray absorption spectral study of ferric high spin hemeproteins: XANES evidence for coordination structure of the heme iron. J. Am. Chem. Soc. 112:2921-2924.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2921-2924
    • Shiro, Y.1    Sato, F.2    Suzuki, T.3    Izuka, T.4    Matsushita, T.5    Oyanagi, H.6
  • 27
    • 80053229547 scopus 로고
    • Hemin intercalated in micellar cetyltrimethylammoniumbromide and Triton X-100. A kinetic, spectral and equilibrium study with cyanide
    • Simplicio, J. 1972. Hemin intercalated in micellar cetyltrimethylammoniumbromide and Triton X-100. A kinetic, spectral and equilibrium study with cyanide. Biochemistry. 11:2525-2534.
    • (1972) Biochemistry , vol.11 , pp. 2525-2534
    • Simplicio, J.1
  • 28
    • 0016825618 scopus 로고
    • Resonance Raman spectroscopic studies of heme proteins
    • Spiro, T. G. 1975. Resonance Raman spectroscopic studies of heme proteins. Biochim. Biophys. Acta. 416:169-187.
    • (1975) Biochim. Biophys. Acta , vol.416 , pp. 169-187
    • Spiro, T.G.1
  • 29
    • 0016998013 scopus 로고
    • Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogues
    • Spiro, T. G., and J. M. Burke. 1976. Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogues. J. Am. Chem. Soc. 98:5482-5489.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 5482-5489
    • Spiro, T.G.1    Burke, J.M.2
  • 30
    • 0002179084 scopus 로고
    • Resonance Raman spectroscopy of metalloporphyrins
    • T. G. Spiro, editor. Wiley Interscience, New York
    • Spiro, T. G., and X. Y. Li. 1988. Resonance Raman spectroscopy of metalloporphyrins. In Biological Application of Raman Spectroscopy, Vol. III. T. G. Spiro, editor. Wiley Interscience, New York. 1-37.
    • (1988) Biological Application of Raman Spectroscopy , vol.3 , pp. 1-37
    • Spiro, T.G.1    Li, X.Y.2
  • 31
    • 0000732729 scopus 로고    scopus 로고
    • Resonance Raman scattering: A probe for heme protein-bound nitric oxide
    • M. Feelisch and J. S. Stamler, editors. John Wiley and Sons, New York
    • Wang, J., W. S. Caughey, and D. L. Rousseau. 1996. Resonance Raman scattering: a probe for heme protein-bound nitric oxide. In Methods in Nitric Oxide Research. M. Feelisch and J. S. Stamler, editors. John Wiley and Sons, New York. 427-454.
    • (1996) Methods in Nitric Oxide Research , pp. 427-454
    • Wang, J.1    Caughey, W.S.2    Rousseau, D.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.