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配体与缺乏远端组氨酸的血红素蛋白结合。来自加州海兔的肌红蛋白(缬氨酸(E7))。

Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)).

作者信息

Bellelli A, Blackmore R S, Gibson Q H

机构信息

Centro di Biologie Molecolare del Consiglio Nationale delle Ricerche, Universitá La Sapienza, Roma, Italy.

出版信息

J Biol Chem. 1990 Aug 15;265(23):13595-600.

PMID:2380176
Abstract

The time course of ligand recombination to the myoglobin from Aplysia limacina, which has Val(E7), was measured following photolysis by flashes of 35 ps to 300 ns with a time resolution of 10 ps or 1 ns. CO shows only biomolecular recombination. O2 has a small geminate reaction with a half-time of tens of picoseconds, but no nanosecond geminate reaction. NO has two picosecond relaxations with half-times of 70 ps (15%) and 1 ns (80%) and one nanosecond relaxation with a half-time of 4.6 ns. The biomolecular rates for O2 and NO are the same: 2 x 10(7) M-1 s-1. Methyl and ethyl isonitriles have a geminate reaction with a half-time of 35 ps. Ethyl isonitrile has, in addition, a nanosecond relaxation (25%) with a half-time of 100 ns. t-Butyl isonitrile has four geminate relaxations (10 ps, 35 ps, 1 ns, and 1 microseconds). Analysis of the results suggests much easier movement of ligand between the heme pocket and the exterior than in sperm whale myoglobin (His(E7]. The reactivity of the heme is little different, placing the effect of the differences from sperm whale myoglobin on the distal side of the heme.

摘要

对来自加利福尼亚海兔(含有缬氨酸(E7))的肌红蛋白进行配体重组的时间进程进行了测量,在35皮秒至300纳秒的闪光光解后,时间分辨率为10皮秒或1纳秒。一氧化碳仅显示双分子重组。氧气有一个半衰期为几十皮秒的小双分子反应,但没有纳秒级双分子反应。一氧化氮有两个皮秒级弛豫,半衰期分别为70皮秒(15%)和1纳秒(80%),以及一个半衰期为4.6纳秒的纳秒级弛豫。氧气和一氧化氮的双分子反应速率相同:2×10⁷ M⁻¹ s⁻¹。甲基和乙基异腈有一个半衰期为35皮秒的双分子反应。此外,乙基异腈还有一个半衰期为100纳秒的纳秒级弛豫(25%)。叔丁基异腈有四个双分子弛豫(10皮秒、35皮秒、1纳秒和1微秒)。结果分析表明,与抹香鲸肌红蛋白(组氨酸(E7))相比,配体在血红素口袋和外部之间的移动要容易得多。血红素的反应性差异不大,这表明与抹香鲸肌红蛋白的差异作用于血红素的远端。

相似文献

1
Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)).配体与缺乏远端组氨酸的血红素蛋白结合。来自加州海兔的肌红蛋白(缬氨酸(E7))。
J Biol Chem. 1990 Aug 15;265(23):13595-600.
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Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques.使用定点诱变和激光光解技术分析配体与抹香鲸肌红蛋白结合的动力学障碍。
J Biol Chem. 1990 Nov 15;265(32):20007-20.
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The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin.E7位(第64位残基)氨基酸取代对配体与抹香鲸肌红蛋白结合动力学的影响。
J Biol Chem. 1990 Feb 25;265(6):3168-76.
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Proteins. 1995 Aug;22(4):322-39. doi: 10.1002/prot.340220404.
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A kinetic description of ligand binding to sperm whale myoglobin.
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Interactions among residues CD3, E7, E10, and E11 in myoglobins: attempts to simulate the ligand-binding properties of Aplysia myoglobin.肌红蛋白中CD3、E7、E10和E11残基之间的相互作用:模拟海兔肌红蛋白配体结合特性的尝试。
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Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin.对海兔肌红蛋白中组氨酸(E7)进行工程改造会影响血红素反应性的调控。
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Contributions of residue 45(CD3) and heme-6-propionate to the biomolecular and geminate recombination reactions of myoglobin.残基45(CD3)和血红素-6-丙酸酯对肌红蛋白生物分子和双分子复合反应的贡献。
Biochemistry. 1991 May 14;30(19):4697-705. doi: 10.1021/bi00233a009.
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New transient species of sperm whale myoglobin in photodissociation of dioxygen from oxymyoglobin.在氧合肌红蛋白的双氧光解离过程中出现的抹香鲸肌红蛋白新瞬态物种。
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Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants.远端口袋残基影响肌红蛋白中皮秒级配体重组。29位突变体的实验与分子动力学研究。
J Biol Chem. 1992 Nov 5;267(31):22022-34.

引用本文的文献

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Full kinetics of CO entry, internal diffusion, and exit in myoglobin from transition-path theory simulations.基于过渡路径理论模拟的肌红蛋白中一氧化碳进入、内部扩散和排出的完整动力学。
J Am Chem Soc. 2015 Mar 4;137(8):3041-50. doi: 10.1021/ja512484q. Epub 2015 Feb 23.
2
Atomic level computational identification of ligand migration pathways between solvent and binding site in myoglobin.肌红蛋白中溶剂与结合位点之间配体迁移途径的原子水平计算识别。
Proc Natl Acad Sci U S A. 2008 Jul 8;105(27):9204-9. doi: 10.1073/pnas.0710825105. Epub 2008 Jul 1.