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首页> 外文期刊>Biochemistry >A Specific Interaction of L-Tryptophan with CO of CO-Bound Indoleamine 2,3-Dioxygenase Identified by Resonance Raman Spectroscopy
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A Specific Interaction of L-Tryptophan with CO of CO-Bound Indoleamine 2,3-Dioxygenase Identified by Resonance Raman Spectroscopy

机译：共振拉曼光谱法鉴定L-色氨酸与CO结合的吲哚胺2,3-双加氧酶的CO的特异性相互作用

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摘要

Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme which catalyzes dioxygenation of L-Trpn(tryptophan), yielding N-formylkynurenine. IDO thus plays a key role in L-Trp catabolism in mammals. Innthe present study, resonance Raman (RR) spectra of the reduced carbon monoxide- (CO-) bound form ofnIDO were measured in order to gain insights into the active site environment of O2. Binding of CO to L-Trp-nbound IDO causes a significant change in the electronic and RR spectra of the heme, indicating that the π*norbitals of the carbon atomof COinteract with π orbitals of Fe and the porphyrin.On the other hand, bindingnof CO to D-Trp-bound IDO does not induce the same change. This is also the case with substrate-free IDO.nBased on the distinct absorption spectra and RR bands of the vibrational signature of CO (ν(CO), δ(FeCO),nand ν(Fe-CO)) of the L-Trp-bound species relative to the other two species, it is confirmed that stericallynconstrained geometry of the Fe-O-O unit exists as previously reported (Terentis, A. C., et al. (2002) J. Biol.nChem. 277, 15788-15794). In contrast, binding of D-Trp does not induce such constraint. The comparablenvalues of Vmax reported for L-Trp and D-Trp are interpreted as a result of a change in the rate-limiting step innthe reaction cycle of the enzyme induced by the D-enantiomer relative to the L-enantiomer. Enhancements ofnthe overtone and the combination Raman modes of the Fe-CO stretching vibration are evident. Thenanharmonicity of the Fe-COstretching oscillator is significantly higher than those of oxygen carrier proteins.nThis is a specific character of IDO and might be responsible for the unique reactivity of this enzyme.
机译：吲哚胺2,3-双加氧酶（IDO）是一种血红素酶，可催化L-Trpn（色氨酸）的双加氧反应，生成N-甲酰基kynurenine。因此，IDO在哺乳动物的L-Trp分解代谢中起关键作用。在本研究中，测量了还原的一氧化碳-（CO-）结合形式的nIDO的共振拉曼（RR）光谱，以便深入了解O2的活性位点环境。 CO与L-Trp-nbound IDO的结合会导致血红素的电子光谱和RR光谱发生显着变化，表明CO的碳原子的π*轨道与Fe和卟啉的π轨道相互作用。 CO与D-Trp结合的IDO不会引起相同的变化。无底物IDO也是这种情况。n基于L-Trp的CO（ν（CO），δ（FeCO），n和ν（Fe-CO））的振动特征的不同吸收光谱和RR带相对于其他两个物种而言，与先前结合的物种相比，已经证实Fe-OO单元的空间上受约束的几何形状如先前报道的那样存在（Terentis，AC等人（2002）J.Biol.nChem.277，15788-15794）。相反，D-Trp的结合不会引起这种约束。对于L-Trp和D-Trp报道的Vmax的可比较值被解释为是由D-对映体相对于L-对映体诱导的酶的反应循环中的限速步骤改变的结果。 Fe-CO拉伸振动的泛音和组合拉曼模式的增强是明显的。 Fe-CO伸展振荡器的南谐性显着高于氧载体蛋白。n这是IDO的特有特征，可能是该酶独特的反应性的原因。

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  • 来源
    《Biochemistry》 |2010年第47期|p.10081-10088|共8页
  • 作者

    Sachiko Yanagisawa Hiroshi Sugimoto Yoshitsugu Shiro and Takashi Ogura;

  • 作者单位

    ‡Department of Life Science and Picobiology Institute, Graduate School of Life Science, University of Hyogo, Koto 3-2-1,Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan, and §Biometal Science Laboratory, RIKEN SPring-8 Center, Koto 1-1-1,Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan;

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