通过激光光解研究血红蛋白构象变化的动力学。
The kinetics of conformational changes in hemoglobin, studied by laser photolysis.
作者信息
Alpert B, Banerjee R, Lindqvist L
出版信息
Proc Natl Acad Sci U S A. 1974 Feb;71(2):558-62. doi: 10.1073/pnas.71.2.558.
Abstract
Photolysis of carbon monoxide and oxygen derivatives of hemoglobin by a short laser pulse produces a transient species that rapidly decays to normal deoxyhemoglobin. The effect, which is also observed on single chain proteins and on noncooperative aggregated forms, has been interpreted as corresponding to structural changes in the heme pocket on ligand dissociation. The decay of the transient species follows first-order kinetics with constants ranging from 0.8 to 1.8 x 10(7) sec(-1). In cooperative hemoglobins, the kinetic constants are pH-dependent, though remaining first- or pseudo first-order at all wavelengths. This shows the close linkage of tertiary and quaternary structure changes in normal hemoglobin.
摘要
短激光脉冲对血红蛋白的一氧化碳和氧衍生物进行光解会产生一种瞬态物质，该物质会迅速衰减为正常的脱氧血红蛋白。这种效应在单链蛋白质和非协同聚集形式上也能观察到，被解释为配体解离时血红素口袋结构的变化。瞬态物质的衰减遵循一级动力学，速率常数范围为0.8至1.8×10⁷秒⁻¹。在协同血红蛋白中，动力学常数依赖于pH值，尽管在所有波长下仍保持一级或准一级。这表明正常血红蛋白中三级和四级结构变化紧密相关。
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本文引用的文献
1
The Oxygen Tension of Arterial Blood.动脉血的氧张力
J Physiol. 1896 Dec 3;20(6):497-520. doi: 10.1113/jphysiol.1896.sp000634.
2
THE KINETICS OF THE BOHR EFFECT IN THE REACTION OF HUMAN HEMOGLOBIN WITH CARBON MONOXIDE.人血红蛋白与一氧化碳反应中玻尔效应的动力学
J Biol Chem. 1965 May;240:2262-4.
3
4
The photochemical formation of a quickly reacting form of haemoglobin.血红蛋白快速反应形式的光化学形成。
Biochem J. 1959 Feb;71(2):293-303. doi: 10.1042/bj0710293.
5
An apparatus for flash photolysis and its application to the reactions of myoglobin with gases.一种用于闪光光解的装置及其在肌红蛋白与气体反应中的应用。
J Physiol. 1956 Oct 29;134(1):112-22. doi: 10.1113/jphysiol.1956.sp005627.
6
The determination of the individual equilibrium constants of the four intermediate reactions between oxygen and sheep haemoglobin.氧气与羊血红蛋白之间四个中间反应的各个平衡常数的测定。
Proc R Soc Lond B Biol Sci. 1955 Aug 16;144(914):29-54. doi: 10.1098/rspb.1955.0032.
7
Observations on rapidly reacting hemoglobin.关于快速反应血红蛋白的观察
J Biol Chem. 1967 Oct 25;242(20):4678-81.
8
Studies on the quantum yields of the photodissociation of carbon monoxide from hemoglobin and myoglobin.关于血红蛋白和肌红蛋白中一氧化碳光解离量子产率的研究。
Biochemistry. 1967 Apr;6(4):1216-22. doi: 10.1021/bi00856a035.
9
Single-crystal spectra of ferrimyoglobin complexes in polarized light.
J Chem Phys. 1968 Aug 1;49(3):985-95. doi: 10.1063/1.1670263.
10
Stereochemistry of cooperative effects in haemoglobin.血红蛋白协同效应的立体化学
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