Christian A Totoiu, Alec H Follmer, Paul H Oyala, Ryan G Hadt
{"title":"用 Fe2S2 金属蛋白探测生物无机电子自旋退相干机制","authors":"Christian A Totoiu, Alec H Follmer, Paul H Oyala, Ryan G Hadt","doi":"10.1021/acs.jpcb.4c06186","DOIUrl":null,"url":null,"abstract":"<p><p>Recent efforts have sought to develop paramagnetic molecular quantum bits (qubits) as a means to store and manipulate quantum information. Emerging structure-property relationships have shed light on electron spin decoherence mechanisms. While insights within molecular quantum information science have derived from synthetic systems, biomolecular platforms would allow for the study of decoherence phenomena in more complex chemical environments and further leverage molecular biology and protein engineering approaches. Here we have employed the exchange-coupled <i>S</i><sub>T</sub> = 1/2 Fe<sub>2</sub>S<sub>2</sub> active site of putidaredoxin, an electron transfer metalloprotein, as a platform for fundamental mechanistic studies of electron spin decoherence toward spin-based biological quantum sensing. At low temperatures, decoherence rates were anisotropic, reflecting a hyperfine-dominated decoherence mechanism, standing in contrast to the anisotropy of molecular systems observed previously. This mechanism provided a pathway for probing spatial effects on decoherence, such as protein vs solvent contributions. Furthermore, we demonstrated spatial sensitivity to single point mutations via site-directed mutagenesis and temporal sensitivity for monitoring solvent isotope exchange. Thus, this study demonstrates a step toward the design and construction of biomolecular quantum sensors.</p>","PeriodicalId":60,"journal":{"name":"The Journal of Physical Chemistry B","volume":null,"pages":null},"PeriodicalIF":2.8000,"publicationDate":"2024-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Probing Bioinorganic Electron Spin Decoherence Mechanisms with an Fe<sub>2</sub>S<sub>2</sub> Metalloprotein.\",\"authors\":\"Christian A Totoiu, Alec H Follmer, Paul H Oyala, Ryan G Hadt\",\"doi\":\"10.1021/acs.jpcb.4c06186\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Recent efforts have sought to develop paramagnetic molecular quantum bits (qubits) as a means to store and manipulate quantum information. Emerging structure-property relationships have shed light on electron spin decoherence mechanisms. While insights within molecular quantum information science have derived from synthetic systems, biomolecular platforms would allow for the study of decoherence phenomena in more complex chemical environments and further leverage molecular biology and protein engineering approaches. Here we have employed the exchange-coupled <i>S</i><sub>T</sub> = 1/2 Fe<sub>2</sub>S<sub>2</sub> active site of putidaredoxin, an electron transfer metalloprotein, as a platform for fundamental mechanistic studies of electron spin decoherence toward spin-based biological quantum sensing. At low temperatures, decoherence rates were anisotropic, reflecting a hyperfine-dominated decoherence mechanism, standing in contrast to the anisotropy of molecular systems observed previously. This mechanism provided a pathway for probing spatial effects on decoherence, such as protein vs solvent contributions. Furthermore, we demonstrated spatial sensitivity to single point mutations via site-directed mutagenesis and temporal sensitivity for monitoring solvent isotope exchange. Thus, this study demonstrates a step toward the design and construction of biomolecular quantum sensors.</p>\",\"PeriodicalId\":60,\"journal\":{\"name\":\"The Journal of Physical Chemistry B\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.8000,\"publicationDate\":\"2024-10-11\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Journal of Physical Chemistry B\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://doi.org/10.1021/acs.jpcb.4c06186\",\"RegionNum\":2,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Journal of Physical Chemistry B","FirstCategoryId":"1","ListUrlMain":"https://doi.org/10.1021/acs.jpcb.4c06186","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
引用次数: 0
摘要
最近,人们一直在努力开发顺磁分子量子位(量子位),作为存储和操纵量子信息的一种手段。新出现的结构-性质关系揭示了电子自旋退相干机制。虽然分子量子信息科学的见解来自于合成系统,但生物分子平台将允许在更复杂的化学环境中研究退相干现象,并进一步利用分子生物学和蛋白质工程方法。在这里,我们以电子传递金属蛋白--putidaredoxin 的交换耦合 ST = 1/2 Fe2S2 活性位点为平台,对电子自旋退相干现象进行基础机理研究,以实现基于自旋的生物量子传感。在低温条件下,退相干速率是各向异性的,反映了一种超精细主导的退相干机制,与之前观察到的分子系统的各向异性形成鲜明对比。这种机制为探测退相干的空间效应(如蛋白质与溶剂的贡献)提供了一种途径。此外,我们还通过定点突变证明了对单点突变的空间敏感性,以及监测溶剂同位素交换的时间敏感性。因此,这项研究向设计和构建生物分子量子传感器迈出了一步。
Probing Bioinorganic Electron Spin Decoherence Mechanisms with an Fe2S2 Metalloprotein.
Recent efforts have sought to develop paramagnetic molecular quantum bits (qubits) as a means to store and manipulate quantum information. Emerging structure-property relationships have shed light on electron spin decoherence mechanisms. While insights within molecular quantum information science have derived from synthetic systems, biomolecular platforms would allow for the study of decoherence phenomena in more complex chemical environments and further leverage molecular biology and protein engineering approaches. Here we have employed the exchange-coupled ST = 1/2 Fe2S2 active site of putidaredoxin, an electron transfer metalloprotein, as a platform for fundamental mechanistic studies of electron spin decoherence toward spin-based biological quantum sensing. At low temperatures, decoherence rates were anisotropic, reflecting a hyperfine-dominated decoherence mechanism, standing in contrast to the anisotropy of molecular systems observed previously. This mechanism provided a pathway for probing spatial effects on decoherence, such as protein vs solvent contributions. Furthermore, we demonstrated spatial sensitivity to single point mutations via site-directed mutagenesis and temporal sensitivity for monitoring solvent isotope exchange. Thus, this study demonstrates a step toward the design and construction of biomolecular quantum sensors.
期刊介绍:
An essential criterion for acceptance of research articles in the journal is that they provide new physical insight. Please refer to the New Physical Insights virtual issue on what constitutes new physical insight. Manuscripts that are essentially reporting data or applications of data are, in general, not suitable for publication in JPC B.