Department of Chemistry, School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan.
Analyst. 2016 Aug 15;141(17):5020-36. doi: 10.1039/c6an01009a.
In this review article, we discuss surface-enhanced resonance Raman scattering (SERRS) studies of hemeproteins such as myoglobin, hemoglobin, and cytochrome on various metal substrates; for example, colloidal silver nanoparticles coated with and without self-assembled monolayers (SAM), a roughened silver electrode protected with and without SAM, a sharp silver tip, and colloidal gold nanoparticles coated with and without SAM. Moreover, we classify the studies in terms of an excitation wavelength; namely, excitation at the B- (Soret) band, Q- (α and β) band, and in the near infrared (NIR) range. In the SERRS studies with B band excitation, it has been shown that the hemeprotein on a silver surface takes a non-native form through detachment from the heme pocket in the protein. With Q band excitation, on the other hand, the change in SERRS has been explained by the orientation of the hemeprotein on the surface. Even by excitation in the NIR range, the peak positions are consistent with the assignment of the major vibrational modes of heme despite there being no resonance Raman effect. Thus, the SERRS of hemeproteins is influenced by a resonance Raman effect, LSPR, and interactions with the metal surface such as structural changes, orientation, and selective adsorption. Moreover, we discuss how SERRS has been applied to complicated biological systems such as living cells containing hemeprotein. For mitochondria, a change of the oxidation-state was observed by the electron transport chain in the cell and at different positions. As an example of a biomedical application of SERRS, the sensitive detection of malaria is presented.
在这篇综述文章中，我们讨论了血蛋白质（如肌红蛋白、血红蛋白和细胞色素）在各种金属基底上的表面增强共振拉曼散射（SERRS）研究；例如，用和不用自组装单层（SAM）涂覆的胶体银纳米粒子、用和不用 SAM 保护的粗糙银电极、尖锐的银尖端以及用和不用 SAM 涂覆的胶体金纳米粒子。此外，我们根据激发波长对这些研究进行了分类；即，在 B-（Soret）带、Q-（α 和 β）带和近红外（NIR）范围内激发。在 B 带激发的 SERRS 研究中，已经表明银表面上的血红素蛋白通过从蛋白质的血红素口袋中脱离而呈现非天然形式。另一方面，在用 Q 带激发时，SERRS 的变化可以通过表面上血红素蛋白的取向来解释。即使在近红外范围内激发，尽管没有共振拉曼效应，但峰位置与血红素主要振动模式的分配一致。因此，血红素蛋白的 SERRS 受到共振拉曼效应、LSPR 和与金属表面的相互作用（如结构变化、取向和选择性吸附）的影响。此外，我们讨论了 SERRS 如何应用于包含血红素蛋白的复杂生物系统，如活细胞。对于线粒体，可以通过细胞内的电子传递链以及在不同位置观察到氧化态的变化。作为 SERRS 在生物医学中的一个应用实例，我们提出了对疟疾的敏感检测。
