Probing Cytochrome c Folding Transitions upon Phototriggered Environmental Perturbations Using Time-Resolved X-ray Scattering.

Probing Cytochrome c Folding Transitions upon Phototriggered Environmental Perturbations Using Time-Resolved X-ray Scattering.
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使用时间分辨的X射线散射探测在光触发环境扰动上进行细胞色素C折叠跃迁。

DOI:
10.1021/acs.jpcb.8b03354
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发表时间:
2018-05-24
期刊:
The journal of physical chemistry. B
影响因子:
--
通讯作者:
Chen LX
Chen LX
中科院分区:
其他
文献类型:
--
作者:
Rimmerman D;Leshchev D;Hsu DJ;Hong J;Abraham B;Henning R;Kosheleva I;Chen LX

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Direct tracking of protein structural dynamics during folding–unfolding processes is important for understanding the roles of hierarchic structural factors in the formation of functional proteins. Using cytochrome c (cyt c) as a platform, we investigated its structural dynamics durin folding processes triggered by local environmental changes (i.e., pH or heme iron center oxidation/spin/ligation states)with time-resolved X-ray solution scattering measurements. Starting from partially unfolded cyt c, a sudden pH drop initiated by light excitation of a photoacid caused a structural contraction in microseconds, followed by active site restructuring and unfolding in milliseconds. In contrast, the reduction of iron in the heme via photoinduced electron transfer did not affect conformational stability at short timescales (<1 ms),despite active site coordination geometry changes. These results demonstrate how different environmental perturbations can change the nature of interaction between the active site and protein conformation, even within the same metalloprotein, which will subsequently affect the folding structural dynamics.
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