一个用赫茨菲尔德-斯坦利形式表示的扩展的莫诺德-怀曼-尚热模型，应用于虹鳟血红蛋白IV的氧和一氧化碳结合曲线。
An extended Monod-Wyman-Changeaux-model expressed in terms of the Herzfeld-Stanley formalism applied to oxygen and carbonmonoxide binding curves of hemoglobin trout IV.
作者信息
Schweitzer-Stenner R, Dreybrodt W
机构信息
University of Bremen, FB 1-Physics Department, Federal Republic of Germany.
出版信息
Biophys J. 1989 Apr;55(4):691-701. doi: 10.1016/S0006-3495(89)82868-1.
Abstract
An extended Monod, Wyman, Changeaux (MWC)-model, the mathematical basis of which had been formulated by Herzfeld and Stanley (J. Mol. Blol. 82:231. 1974.) was used to fit oxygen and CO-binding curves of hemoglobin trout IV measured at different pH-values between pH = 8.0 and 6.0. From this calculation one obtains that even the fully liganded molecule exhibits a R----T quaternary transition upon approaching the acid pH-region. In the case of O2-binding, the cooperativity becomes negative below pH = 6.5. This can be related to the difference between the equilibrium constants of proton binding to the alpha- and beta-subunits. Furthermore, it can be shown that the interaction between the quaternary T----R- and the tertiary t----r-transitions is different for the alpha- and beta-subunits.
摘要
一个扩展的莫诺德-怀曼-钱考克斯（MWC）模型，其数学基础由赫茨费尔德和斯坦利（《分子生物学杂志》82:231. 1974）提出，用于拟合在pH = 8.0至6.0之间不同pH值下测量的虹鳟血红蛋白IV的氧结合曲线和一氧化碳结合曲线。通过该计算得出，即使是完全结合配体的分子在接近酸性pH区域时也会发生R----T四级转变。在氧气结合的情况下，在pH = 6.5以下协同性变为负值。这可能与质子结合到α-和β-亚基的平衡常数差异有关。此外，可以表明四级T----R转变和三级t----r转变之间的相互作用对于α-和β-亚基是不同的。
相似文献
1
An extended Monod-Wyman-Changeaux-model expressed in terms of the Herzfeld-Stanley formalism applied to oxygen and carbonmonoxide binding curves of hemoglobin trout IV.一个用赫茨菲尔德-斯坦利形式表示的扩展的莫诺德-怀曼-尚热模型，应用于虹鳟血红蛋白IV的氧和一氧化碳结合曲线。
Biophys J. 1989 Apr;55(4):691-701. doi: 10.1016/S0006-3495(89)82868-1.
2
Detection of the heme perturbations caused by the quaternary R----T transition in oxyhemoglobin trout IV by resonance Raman scattering.通过共振拉曼散射检测鳟鱼血红蛋白IV中氧合血红蛋白四级结构从R态到T态转变引起的血红素扰动。
Biophys J. 1989 Apr;55(4):703-12. doi: 10.1016/S0006-3495(89)82869-3.
3
Functional properties of partially oxidized trout hemoglobins.部分氧化的鳟鱼血红蛋白的功能特性
Biochim Biophys Acta. 1977 Jan 25;490(1):171-7. doi: 10.1016/0005-2795(77)90117-9.
4
Dynamics of the quaternary conformational change in trout hemoglobin.虹鳟血红蛋白四级结构构象变化的动力学
Biochemistry. 1991 Jul 2;30(26):6583-98. doi: 10.1021/bi00240a031.
5
Thermodynamic analysis of carbon monoxide binding by hemoglobin trout I.血红蛋白鳟鱼I对一氧化碳结合的热力学分析。
Biophys Chem. 1979 Mar;9(3):235-44. doi: 10.1016/0301-4622(79)85006-1.
6
Photodissociation of CO and O2 from alpha and beta hemoglobin chains studied by using picosecond absorption spectroscopy.通过皮秒吸收光谱法研究α和β血红蛋白链中CO和O₂的光解离。
Biophys J. 1987 Nov;52(5):885-9. doi: 10.1016/S0006-3495(87)83282-4.
7
Heats of carbon monoxide binding by hemoglobin M Iwate.血红蛋白岩手型与一氧化碳结合的热效应
Biochemistry. 1975 Oct 21;14(21):4584-9. doi: 10.1021/bi00692a005.
8
The carbon monoxide-oxygen partition coefficient of isolated alpha and beta chains from hemoglobin A0.血红蛋白A0中分离出的α链和β链的一氧化碳-氧气分配系数。
Biopolymers. 1986 Aug;25(8):1381-4. doi: 10.1002/bip.360250802.
9
The kinetics and equilibria of squirrel-fish hemoglobin. A Root effect hemoglobin complicated by large subunit heterogeneity.松鼠鱼血红蛋白的动力学与平衡。一种因大亚基异质性而复杂化的根效应血红蛋白。
Biochim Biophys Acta. 1978 Mar 28;533(1):120-9. doi: 10.1016/0005-2795(78)90555-x.
10
Allosteric kinetics and equilibria differ for carbon monoxide and oxygen binding to hemoglobin.一氧化碳和氧气与血红蛋白结合的变构动力学及平衡有所不同。
Biophys J. 1990 Aug;58(2):333-40. doi: 10.1016/S0006-3495(90)82380-8.
引用本文的文献
1
Raman dispersion spectroscopy probes heme distortions in deoxyHb-trout IV involved in its T-state Bohr effect.喇曼光谱分散技术探测脱氧 Hb-鳟鱼 IV 中的亚铁血红素构象变化，这与它 T 态的波尔效应有关。
Biophys J. 1993 Apr;64(4):1194-209. doi: 10.1016/S0006-3495(93)81485-1.
2
Structural heterogeneity of the Fe(2+)-N epsilon (HisF8) bond in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode.通过拉曼活性铁-组氨酸伸缩模式探测的各种血红蛋白和肌红蛋白衍生物中Fe(2+)-Nε(HisF8)键的结构异质性
Biophys J. 1993 Oct;65(4):1470-85. doi: 10.1016/S0006-3495(93)81216-5.
3
The influence of structural variations in the F- and FG-helix of the beta-subunit modified oxyHb-NES on the heme structure detected by resonance Raman spectroscopy.β亚基修饰的氧合血红蛋白核输出信号（oxyHb-NES）中F螺旋和FG螺旋结构变异对通过共振拉曼光谱检测的血红素结构的影响。
Eur Biophys J. 1989;17(2):87-100. doi: 10.1007/BF00257106.
4
Detection of the heme perturbations caused by the quaternary R----T transition in oxyhemoglobin trout IV by resonance Raman scattering.通过共振拉曼散射检测鳟鱼血红蛋白IV中氧合血红蛋白四级结构从R态到T态转变引起的血红素扰动。
Biophys J. 1989 Apr;55(4):703-12. doi: 10.1016/S0006-3495(89)82869-3.
5
Fractal mechanisms for the allosteric effects of proteins and enzymes.蛋白质和酶变构效应的分形机制。
Biophys J. 1990 Nov;58(5):1313-20. doi: 10.1016/S0006-3495(90)82472-3.
6
pH-induced conformational changes of the Fe(2+)-N epsilon (His F8) linkage in deoxyhemoglobin trout IV detected by the Raman active Fe(2+)-N epsilon (His F8) stretching mode.通过拉曼活性的Fe(2+)-Nε(组氨酸F8)伸缩模式检测到的脱氧血红蛋白鳟鱼IV中Fe(2+)-Nε(组氨酸F8)键合的pH诱导构象变化。
Biophys J. 1992 Jan;61(1):31-41. doi: 10.1016/S0006-3495(92)81813-1.
本文引用的文献
1
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.关于别构转变的本质：一个合理的模型。
J Mol Biol. 1965 May;12:88-118. doi: 10.1016/s0022-2836(65)80285-6.
2
Stereochemistry of cooperative effects in fish an amphibian haemoglobins.鱼类和两栖类血红蛋白协同效应的立体化学
Nature. 1982 Sep 30;299(5882):421-6. doi: 10.1038/299421a0.
3
Structure of human oxyhaemoglobin at 2.1 A resolution.人氧合血红蛋白在2.1埃分辨率下的结构。
J Mol Biol. 1983 Nov 25;171(1):31-59. doi: 10.1016/s0022-2836(83)80313-1.
4
Comparison of experimental binding data and theoretical models in proteins containing subunits.含亚基蛋白质中实验结合数据与理论模型的比较。
Biochemistry. 1966 Jan;5(1):365-85. doi: 10.1021/bi00865a047.
5
Stereochemistry of cooperative effects in haemoglobin.血红蛋白协同效应的立体化学
Nature. 1970 Nov 21;228(5273):726-39. doi: 10.1038/228726a0.
6
A general approach to co-operativity and its application to the oxygen equilibrium of hemoglobin and its effectors.协同性的一般方法及其在血红蛋白氧平衡及其效应物中的应用。
J Mol Biol. 1974 Jan 15;82(2):231-65. doi: 10.1016/0022-2836(74)90343-x.
7
A mathematical model for structure-function relations in hemoglobin.血红蛋白结构-功能关系的数学模型。
J Mol Biol. 1972 Dec 14;72(1):163-97. doi: 10.1016/0022-2836(72)90077-0.
8
Heme-apoprotein interaction in the modified oxyhemoglobin-bis(N-maleimidomethyl)ether and in oxyhemoglobin at high Cl-concentration detected by resonance Raman scattering.通过共振拉曼散射检测在修饰的氧合血红蛋白-双（N-马来酰亚胺甲基）醚以及高氯离子浓度下的氧合血红蛋白中的血红素-载脂蛋白相互作用。
Biochim Biophys Acta. 1985 Aug 23;830(3):224-32. doi: 10.1016/0167-4838(85)90278-x.
9
Thermodynamic characterization of the allosteric transition in trout hemoglobin.鳟鱼血红蛋白变构转变的热力学特征
Eur Biophys J. 1986;13(4):245-9. doi: 10.1007/BF00260371.
10
Detection of the heme perturbations caused by the quaternary R----T transition in oxyhemoglobin trout IV by resonance Raman scattering.通过共振拉曼散射检测鳟鱼血红蛋白IV中氧合血红蛋白四级结构从R态到T态转变引起的血红素扰动。
Biophys J. 1989 Apr;55(4):703-12. doi: 10.1016/S0006-3495(89)82869-3.
Zotero 插件