Direct observation of photolysis-induced tertiary structural changes in hemoglobin

被引:60
作者
Adachi, S
Park, SY
Tame, JRH
Shiro, Y
Shibayama, N
机构
[1] RIKEN, Harima Inst, SPring 8, Sayo, Hyogo 6795148, Japan
[2] Yokohama City Univ, Grad Sch Integrated Sci, Prot Design Lab, Yokohama, Kanagawa 2300045, Japan
[3] Jichi Med Sch, Div Biophys, Dept Physiol, Kawachi, Tochigi 3290498, Japan
关键词
D O I
10.1073/pnas.1230629100
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Human Hb, an alpha(2)beta(2) tetrameric oxygen transport protein that switches from a T (tense) to an R (relaxed) quaternary structure during oxygenation, has long served as a model for studying protein allostery, in general. Time-resolved spectroscopic measurements after photodissociation of CO-liganded Hb have played a central role in exploring both protein dynamical responses and molecular cooperativity, but the direct visualization and the structural consequences of photodeligation have not yet been reported. Here we present an x-ray study of structural changes induced by photodissociation of half-liganded T-state and fully liganded R-state human Hb at cryogenic temperatures (25-35 K). On photodissociation of CO, structural changes involving the heme and the F-helix are more marked in the a subunit than in the beta subunit, and more subtle in the R state than in the T state. Photodeligation causes a significant sliding motion of the T-state beta heme. Our results establish that the structural basis of the low affinity of the T state is radically different between the subunits, because of differences in the packing and chemical tension at the hemes.
引用
收藏
页码:7039 / 7044
页数:6
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共 44 条
  • [1] The RIKEN structural biology beamline II (BL44B2) at the SPring-8
    Adachi, S
    Oguchi, T
    Tanida, H
    Park, SY
    Shimizu, H
    Miyatake, H
    Kamiya, N
    Shiro, Y
    Inoue, Y
    Ueki, T
    Iizuka, T
    [J]. NUCLEAR INSTRUMENTS & METHODS IN PHYSICS RESEARCH SECTION A-ACCELERATORS SPECTROMETERS DETECTORS AND ASSOCIATED EQUIPMENT, 2001, 467 : 711 - 714
  • [2] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY
    BAILEY, S
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 : 760 - 763
  • [3] HEMOGLOBIN - STRUCTURAL-CHANGES RELATED TO LIGAND-BINDING AND ITS ALLOSTERIC MECHANISM
    BALDWIN, J
    CHOTHIA, C
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1979, 129 (02) : 175 - +
  • [4] A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin
    Barrick, D
    Ho, NT
    Simplaceanu, V
    Dahlquist, FW
    Ho, C
    [J]. NATURE STRUCTURAL BIOLOGY, 1997, 4 (01) : 78 - 83
  • [5] COOPERATIVE LIGAND-BINDING OF CROSS-LINKED HEMOGLOBINS AT VERY HIGH-TEMPERATURES
    BELLELLI, A
    IPPOLITI, R
    BRANCACCIO, A
    LENDARO, E
    BRUNORI, M
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1990, 213 (04) : 571 - 574
  • [6] BIS-PYRIDOXAL POLYPHOSPHATES - A NEW CLASS OF SPECIFIC INTRAMOLECULAR CROSSLINKING AGENTS FOR HEMOGLOBIN
    BENESCH, RE
    KWONG, S
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1988, 156 (01) : 9 - 14
  • [7] COUPLED REACTIONS IN HEMOGLOBIN - HEME-GLOBIN AND DIMER-DIMER ASSOCIATION
    BENESCH, RE
    KWONG, S
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (23) : 13785 - 13786
  • [8] Allosteric intermediates in hemoglobin .1. Nanosecond time-resolved circular dichroism spectroscopy
    Bjorling, SC
    Goldbeck, RA
    Paquette, SJ
    Milder, SJ
    Kliger, DS
    [J]. BIOCHEMISTRY, 1996, 35 (26) : 8619 - 8627
  • [9] CARBON-MONOXIDE BINDING TO THE FERROUS CHAINS OF [MN,FE(II)] HYBRID HEMOGLOBINS - PH-DEPENDENCE OF THE CHAIN AFFINITY CONSTANTS ASSOCIATED WITH SPECIFIC HEMOGLOBIN LIGATION PATHWAYS
    BLOUGH, NV
    HOFFMAN, BM
    [J]. BIOCHEMISTRY, 1984, 23 (13) : 2875 - 2882
  • [10] CHATTERJEE R, 1986, J BIOL CHEM, V261, P9929