Fluorescence study of the conformational properties of myoglobin structure. 2. pH- and ligand-induced conformational changes in ferric- and ferrousmyoglobins.
作者： Galina B. POSTNIKOVA , Yuri E. KOMAROV , Elena M. YUMAKOVA
DOI: 10.1111/J.1432-1033.1991.TB16006.X
关键词: Stereochemistry 、 Biophysics 、 Heme 、 Protein structure 、 Hemeprotein 、 Fluorescence spectrometry 、 Fluorescence anisotropy 、 Ligand (biochemistry) 、 Chemistry 、 Myoglobin 、 Metmyoglobin
摘要: Myoglobin is known to be the reference protein that why knowledge of conformational behavior myoglobin-like structure common importance for understanding mechanism functioning. In this work fluorescence was used study pH- and ligand-induced changes in sperm whale myoglobin related structures — apomyoglobin (apo-Mb) complex apo-Mb with protoporphyrin IX (PPIX-apo-Mb) which a iron-free analog Mb. The structural at N-terminal adjacent region were followed by two invariant tryptophans A-helix, Trp7(A5) Trpl4(A12), while those “active site”, heme crevice, emission PPIX. As distinct from non-fluorescing heme, PPIX has an extensive visible spectral region.
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sci-hub.se 参考文章(38)
Eraldo Antonini, Maurizio Brunori, Hemoglobin and myoglobin in their reactions with ligands ,(1971)
R.E. Hirsch, R.L. Nagel, Conformational studies of hemoglobins using intrinsic fluorescence measurements. Journal of Biological Chemistry. ,vol. 256, pp. 1080- 1083 ,(1981) , 10.1016/S0021-9258(19)69925-4
David Puett, The Equilibrium Unfolding Parameters of Horse and Sperm Whale Myoglobin: EFFECTS OF GUANIDINE HYDROCHLORIDE, UREA, AND ACID Journal of Biological Chemistry. ,vol. 248, pp. 4623- 4634 ,(1973) , 10.1016/S0021-9258(19)43709-5
N.N. Ugarova, A.P. Savitski, I.V. Berezin, The protoporphyrin-apoperoxidase complex as a horseradish peroxidase analog Biochimica et Biophysica Acta (BBA) - Enzymology. ,vol. 662, pp. 210- 219 ,(1981) , 10.1016/0005-2744(81)90032-2
Giovanni Colonna, Gaetano Irace, Giuseppe Parlato, Salvatore M. Aloj, Ciro Balestrieri, The effect of evolution on homologous proteins Biochimica et Biophysica Acta (BBA) - Protein Structure. ,vol. 532, pp. 354- 367 ,(1978) , 10.1016/0005-2795(78)90590-1
T. Takano, Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale. Journal of Molecular Biology. ,vol. 110, pp. 537- 568 ,(1977) , 10.1016/S0022-2836(77)80111-3
Tian Yow Tsong, The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation. Journal of Biological Chemistry. ,vol. 249, pp. 1988- 1990 ,(1974) , 10.1016/S0021-9258(19)42881-0
Frances C. Bernstein, Thomas F. Koetzle, Graheme J.B. Williams, Edgar F. Meyer, Michael D. Brice, John R. Rodgers, Olga Kennard, Takehiko Shimanouchi, Mitsuo Tasumi, The Protein Data Bank: a computer-based archival file for macromolecular structures. Journal of Molecular Biology. ,vol. 112, pp. 535- 542 ,(1977) , 10.1016/S0022-2836(77)80200-3
Rhoda Elison Hirsch, R.Suzanne Zukin, Ronald L. Nagel, Intrinsic fluorescence emission of intact oxy hemoglobins. Biochemical and Biophysical Research Communications. ,vol. 93, pp. 432- 439 ,(1980) , 10.1016/0006-291X(80)91096-7
Alan N. Schechter, Charles J. Epstein, Spectral studies on the denaturation of myoglobin. Journal of Molecular Biology. ,vol. 35, pp. 567- 589 ,(1968) , 10.1016/S0022-2836(68)80015-4