血红蛋白中的配体结合过程。通过X射线吸收近边结构光谱研究铁的化学反应性。
Ligand binding processes in hemoglobin. Chemical reactivity of iron studied by XANES spectroscopy.
作者信息
Pin S, Valat P, Cortes R, Michalowicz A, Alpert B
出版信息
Biophys J. 1985 Dec;48(6):997-1001. doi: 10.1016/S0006-3495(85)83862-5.
Abstract
K-absorption edge of coordinated ions exhibits a fine structure (through the use of XANES, or x-ray absorption near edge structures) that reflects the electronic repartition and the chemical reactivity of these ions. Comparative analysis of iron K-absorption-edge shape for hemoglobin derivatives with different ligand affinity suggests strongly that in hemoglobin, iron-forms with high and low affinity are highly improbable.
摘要
配位离子的K吸收边呈现出一种精细结构（通过使用XANES，即X射线吸收近边结构），该结构反映了这些离子的电子分布和化学反应性。对具有不同配体亲和力的血红蛋白衍生物的铁K吸收边形状进行比较分析，强烈表明在血红蛋白中，具有高亲和力和低亲和力的铁形式极不可能存在。
相似文献
1
Ligand binding processes in hemoglobin. Chemical reactivity of iron studied by XANES spectroscopy.血红蛋白中的配体结合过程。通过X射线吸收近边结构光谱研究铁的化学反应性。
Biophys J. 1985 Dec;48(6):997-1001. doi: 10.1016/S0006-3495(85)83862-5.
2
Alteration of heme axial ligands in hemoglobin by organic solvents analyzed by CD, FTIR, and XANES techniques.
Biochemistry. 1991 Mar 19;30(11):2804-10. doi: 10.1021/bi00225a010.
3
Collective motion of iron and exogenous ligands in hemoglobin.
Biochemistry. 1989 Sep 5;28(18):7144-7. doi: 10.1021/bi00444a002.
4
XANES spectroscopy of carp hemoglobin-iron in correlation with the affinity changes of the protein for ligand.鲤鱼血红蛋白铁的X射线吸收近边结构光谱与该蛋白质对配体亲和力变化的相关性
FEBS Lett. 1986 Nov 24;208(2):325-30. doi: 10.1016/0014-5793(86)81043-2.
5
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.
6
Coupling of ferric iron spin and allosteric equilibrium in hemoglobin.血红蛋白中铁离子自旋与别构平衡的偶联
Biophys J. 1991 Oct;60(4):770-6. doi: 10.1016/S0006-3495(91)82111-7.
7
Effect of peroxodisulphate ions on functional behaviour of hemoglobin.过二硫酸盐离子对血红蛋白功能行为的影响。
Gen Physiol Biophys. 1991 Dec;10(6):577-87.
8
Conformational kinetics of triligated hemoglobin.三配位血红蛋白的构象动力学
Biophys J. 1985 Aug;48(2):269-82. doi: 10.1016/S0006-3495(85)83780-2.
9
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.
10
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.
引用本文的文献
1
How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site.纳米颗粒如何修饰吸附的蛋白质：二氧化硅纳米颗粒对血红蛋白活性位点的影响。
Int J Mol Sci. 2023 Feb 11;24(4):3659. doi: 10.3390/ijms24043659.
2
X-ray snapshots reveal conformational influence on active site ligation during metalloprotein folding.X射线快照揭示了金属蛋白折叠过程中构象对活性位点连接的影响。
Chem Sci. 2019 Sep 3;10(42):9788-9800. doi: 10.1039/c9sc02630d. eCollection 2019 Nov 14.
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
LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK.血红蛋白中的关联功能与相互作用：再审视
Adv Protein Chem. 1964;19:223-86. doi: 10.1016/s0065-3233(08)60190-4.
3
Side reactions in the deoxygenation of dilute oxyhaemoglobin solutions by sodium dithionite.连二亚硫酸钠对稀氧合血红蛋白溶液进行脱氧时的副反应
Biochem J. 1957 Sep;67(1):119-24.
4
Nature of haem-haem interaction.血红素-血红素相互作用的本质
Nature. 1972 Jun 30;237(5357):495-9. doi: 10.1038/237495a0.
5
X-ray absorption near edge structure (XANES) for CO, CN and deoxyhaemoglobin: geometrical information.一氧化碳、氰根与脱氧血红蛋白的X射线吸收近边结构（XANES）：几何信息
EMBO J. 1983;2(9):1441-3. doi: 10.1002/j.1460-2075.1983.tb01605.x.
6
Study of haem structure of photo-deligated haemoglobin by picosecond resonance Raman spectra.皮秒共振拉曼光谱法对光解血红蛋白血红素结构的研究
Nature. 1980 Apr 10;284(5756):568-70. doi: 10.1038/284568a0.
7
Interaction of hemoglobin with salts. Effects on the functional properties of human hemoglobin.
J Mol Biol. 1981 Oct 15;152(1):111-29. doi: 10.1016/0022-2836(81)90097-8.
8
Oxygen diffusion through hemoglobin and HbdesFe: quenching of the tryptophan and porphyrin emissions.
FEBS Lett. 1981 Apr 20;126(2):191-4. doi: 10.1016/0014-5793(81)80239-6.
9
Cooperative deoxygenation of haemoglobin: asymmetry of binding and subunit differences.血红蛋白的协同脱氧作用：结合的不对称性和亚基差异
Nature. 1982 Dec 16;300(5893):661-2. doi: 10.1038/300661a0.
10
Asymmetric ligand binding by haemoglobin.血红蛋白的不对称配体结合
Nature. 1982 Dec 16;300(5893):603-7. doi: 10.1038/300603a0.
Zotero 插件