非指数型蛋白质弛豫：肌红蛋白构象变化的动力学
Nonexponential protein relaxation: dynamics of conformational change in myoglobin.
作者信息
Lim M, Jackson T A, Anfinrud P A
机构信息
Department of Chemistry, Harvard University, Cambridge, MA 02138.
出版信息
Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5801-4. doi: 10.1073/pnas.90.12.5801.
Abstract
The picosecond evolution of the tertiary conformation of myoglobin (Mb) after photodissociation of MbCO was investigated at room temperature by probing band III, a weak iron-porphyrin charge-transfer transition near 13,110 cm-1 (763 nm) that is sensitive to the out-of-plane displacement of the iron. Upon photolysis, the iron moves out of the plane of the porphyrin, causing a blue-shift of band III and a concomitant change in the protein conformation. The dynamics for this functionally important motion are highly nonexponential, in agreement with recent molecular dynamics simulations [Kuczera, K., Lambry, J.-C., Martin, J.-L. & Karplus, M. (1993) Proc. Natl. Acad. Sci. USA 90, 5805-5807]. The conformational change likely affects the height of the barrier to ligand rebinding and may explain nonexponential NO rebinding.
摘要
通过探测Ⅲ带，在室温下研究了肌红蛋白（Mb）与一氧化碳（MbCO）光解离后三级构象的皮秒级演化。Ⅲ带是位于13110 cm-1（763 nm）附近的一个弱铁卟啉电荷转移跃迁，对铁的平面外位移敏感。光解时，铁移出卟啉平面，导致Ⅲ带蓝移并伴随蛋白质构象变化。这种功能上重要运动的动力学是高度非指数性的，这与最近的分子动力学模拟结果一致[库泽拉，K.，兰布里，J.-C.，马丁，J.-L.和卡尔普斯，M.（1993年）《美国国家科学院院刊》90，5805 - 5807]。构象变化可能影响配体重新结合的势垒高度，并可能解释非指数性的一氧化氮重新结合。
相似文献
1
Nonexponential protein relaxation: dynamics of conformational change in myoglobin.非指数型蛋白质弛豫：肌红蛋白构象变化的动力学
Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5801-4. doi: 10.1073/pnas.90.12.5801.
2
Nonexponential relaxation after ligand dissociation from myoglobin: a molecular dynamics simulation.配体从肌红蛋白解离后的非指数弛豫：分子动力学模拟
Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5805-7. doi: 10.1073/pnas.90.12.5805.
3
Protein conformational relaxation following photodissociation of CO from carbonmonoxymyoglobin: picosecond circular dichroism and absorption studies.一氧化碳肌红蛋白中CO光解离后的蛋白质构象弛豫：皮秒圆二色性和吸收研究。
Biochemistry. 1991 Apr 16;30(15):3682-92. doi: 10.1021/bi00229a013.
4
Ligand binding to heme proteins: connection between dynamics and function.配体与血红素蛋白的结合：动力学与功能之间的联系。
Biochemistry. 1991 Apr 23;30(16):3988-4001. doi: 10.1021/bi00230a026.
5
Spectroscopic evidence for conformational relaxation in myoglobin.肌红蛋白构象弛豫的光谱学证据。
Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):2902-6. doi: 10.1073/pnas.89.7.2902.
6
Protein conformation-controlled rebinding barrier of NO and its binding trajectories in myoglobin and hemoglobin at room temperature.室温下肌红蛋白和血红蛋白中 NO 的蛋白构象控制再结合势垒及其结合轨迹。
J Phys Chem B. 2012 May 24;116(20):5819-30. doi: 10.1021/jp300176q. Epub 2012 May 11.
7
Photoexcitation dynamics of NO-bound ferric myoglobin investigated by femtosecond vibrational spectroscopy.飞秒振动光谱研究 NO 结合的高铁肌红蛋白的光激发动力学。
J Phys Chem B. 2013 Mar 14;117(10):2850-63. doi: 10.1021/jp400055d. Epub 2013 Mar 4.
8
Different relaxations in myoglobin after photolysis.光解后肌红蛋白的不同弛豫现象。
Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14402-7. doi: 10.1073/pnas.0406062101. Epub 2004 Sep 22.
9
Investigations of optical line shapes and kinetic hole burning in myoglobin.肌红蛋白中光学线形和动态烧孔的研究。
Biochemistry. 1991 Jul 30;30(30):7390-402. doi: 10.1021/bi00244a005.
10
Dynamics of ligand binding to myoglobin.配体与肌红蛋白结合的动力学
Biochemistry. 1975 Dec 2;14(24):5355-73. doi: 10.1021/bi00695a021.
引用本文的文献
1
Two-Dimensional Fluctuation Correlation Spectroscopy (2D-FlucCS): A Method to Determine the Origin of Relaxation Rate Dispersion.二维涨落相关光谱法（2D-FlucCS）：一种确定弛豫速率色散起源的方法。
ACS Meas Sci Au. 2024 Feb 1;4(2):153-162. doi: 10.1021/acsmeasuresciau.3c00048. eCollection 2024 Apr 17.
2
Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering.飞秒 X 射线溶液散射可视化研究同二聚体血红蛋白的超快相干运动和螺旋重排。
Nat Commun. 2021 Jun 16;12(1):3677. doi: 10.1038/s41467-021-23947-7.
3
The Impact of Electron Correlation on Describing QM/MM Interactions in the Attendant Molecular Dynamics Simulations of CO in Myoglobin.电子相关对描述肌红蛋白中 CO 伴随分子动力学模拟中 QM/MM 相互作用的影响。
Sci Rep. 2020 May 22;10(1):8539. doi: 10.1038/s41598-020-65475-2.
4
What Can Be Learned from Nuclear Resonance Vibrational Spectroscopy: Vibrational Dynamics and Hemes.从核共振振动光谱学中可以学到什么：振动动力学与血红素
Chem Rev. 2017 Oct 11;117(19):12532-12563. doi: 10.1021/acs.chemrev.7b00295. Epub 2017 Sep 18.
5
Ultrafast anisotropic protein quake propagation after CO photodissociation in myoglobin.肌红蛋白中CO光解离后超快各向异性蛋白质振动传播
Proc Natl Acad Sci U S A. 2016 Sep 20;113(38):10565-70. doi: 10.1073/pnas.1603539113. Epub 2016 Sep 6.
6
Enzyme transient state kinetics in crystal and solution from the perspective of a time-resolved crystallographer.从时间分辨晶体学家的角度看晶体和溶液中的酶瞬变态动力学。
Struct Dyn. 2014 Mar 27;1(2):024701. doi: 10.1063/1.4869472. eCollection 2014 Mar.
7
Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser.利用X射线自由电子激光观测到的超快肌红蛋白结构动力学
Nat Commun. 2015 Apr 2;6:6772. doi: 10.1038/ncomms7772.
8
Sub-100-ps structural dynamics of horse heart myoglobin probed by time-resolved X-ray solution scattering.通过时间分辨X射线溶液散射探测马心脏肌红蛋白的亚100皮秒结构动力学。
Chem Phys. 2014 Oct 17;422:137-142. doi: 10.1016/j.chemphys.2014.03.004.
9
Kinetic response of a photoperturbed allosteric protein.光扰动变构蛋白的动力学响应。
Proc Natl Acad Sci U S A. 2013 Jul 16;110(29):11725-30. doi: 10.1073/pnas.1306323110. Epub 2013 Jul 1.
10
Complex of myoglobin with phenol bound in a proximal cavity.肌红蛋白与结合在近端腔中的苯酚的复合物。
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1465-71. doi: 10.1107/S1744309112045514. Epub 2012 Nov 19.
本文引用的文献
1
Relaxation dynamics of myoglobin in solution.溶液中肌红蛋白的弛豫动力学
Phys Rev Lett. 1992 Jan 20;68(3):408-411. doi: 10.1103/PhysRevLett.68.408.
2
Nonexponential relaxation after ligand dissociation from myoglobin: a molecular dynamics simulation.配体从肌红蛋白解离后的非指数弛豫：分子动力学模拟
Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5805-7. doi: 10.1073/pnas.90.12.5805.
3
Structure and refinement of oxymyoglobin at 1.6 A resolution.分辨率为1.6埃的氧合肌红蛋白的结构与精修
J Mol Biol. 1980 Oct 5;142(4):531-54. doi: 10.1016/0022-2836(80)90262-4.
4
Polarized absorption and linear dichroism spectroscopy of hemoglobin.血红蛋白的偏振吸收和线性二色性光谱
Methods Enzymol. 1981;76:175-261. doi: 10.1016/0076-6879(81)76126-3.
5
Geminate recombination of carbon monoxide to myoglobin.一氧化碳与肌红蛋白的双分子复合。
J Mol Biol. 1983 May 25;166(3):443-51. doi: 10.1016/s0022-2836(83)80094-1.
6
Ultrafast relaxation in picosecond photolysis of nitrosylhemoglobin.亚硝基血红蛋白皮秒光解中的超快弛豫
J Mol Biol. 1983 Jan 5;163(1):119-28. doi: 10.1016/0022-2836(83)90032-3.
7
Low temperature photodissociation of hemoproteins: carbon monoxide complex of myoglobin and hemoglobin.血红蛋白的低温光解离：肌红蛋白和血红蛋白的一氧化碳复合物
Biochim Biophys Acta. 1974 Nov 5;371(1):126-39. doi: 10.1016/0005-2795(74)90161-5.
8
A calorimetric study of the binding of carbon monoxide to myoglobin.一氧化碳与肌红蛋白结合的量热研究。
Biochemistry. 1972 Mar 14;11(6):1098-101. doi: 10.1021/bi00756a024.
9
Structures of photolyzed carboxymyoglobin.光解羧基肌红蛋白的结构。
Biochemistry. 1985 Dec 31;24(27):7964-70. doi: 10.1021/bi00348a019.
10
Protein states and proteinquakes.蛋白质状态与蛋白质震颤。
Proc Natl Acad Sci U S A. 1985 Aug;82(15):5000-4. doi: 10.1073/pnas.82.15.5000.
Zotero 插件