Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin A and -myoglobin: detection of bound N-O stretching and Fe-NO stretching vibrations from the hexacoordinated NO-heme complex.
Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin A and -myoglobin: detection of bound N-O stretching and Fe-NO stretching vibrations from the hexacoordinated NO-heme complex.
复制标题
亚硝酰血红蛋白 A 和 肌红蛋白中一氧化氮键合的共振拉曼研究：检测六配位 NO-血红素复合物中结合的 N-O 伸缩和 Fe-NO 伸缩振动。
作者：
Tsubaki,M;Yu,NT
Motonari Tsubaki* 和Nai-Teng Yu* 摘要：在406.7 nm激发下，我们观察到亚硝基血红蛋白A和亚硝基肌红蛋白在-1623 cm-1处的束缚v（NO）伸缩共振拉曼增强，表明存在强Soret带下的电荷转移跃迁。还在Soret以及Q带区域中检测到在551 cm-1处的y（Fe-NO）伸缩，这是与氧和碳单氧血红素蛋白中的i/（Fe-02）和y（Fe-CO）伸缩类似的现象。这些铁-配体的振动可能是通过卟啉-* 跃迁共振增强的。当四元结构从R型转换为T型时，一氧化氮（NO）已被用作探针来检测血红蛋白（Hb）中血红素部分的构象变化（Rein等人，1972; Cassoly，1974; Taketa等人，1975;麦克斯韦和考伊，1976;佩鲁茨等人，1976年）。电子顺磁共振（EPR）研究表明，人亚硝基血红蛋白A（亚硝基-HbA）在R结构中。
Motonari Tsubaki* and Nai-Teng Yu* abstract: With excitation at 406.7 nm, we have observed the resonance Raman enhancement of the bound v (NO) stretch at—1623 cm'1 in nitrosylhemoglobin A and nitro-sylmyoglobin, indicating the existence of a charge-transfer transition underlying the strong Soretband. The y (Fe-NO) stretch at 551 cm" 1 has also been detected in the Soret as well as in the Q-band region, a phenomenon similar to the i/(Fe-02) and y (Fe-CO) stretches in oxy and carbon monoxy hemoproteins. It appears that these iron-ligand vibrationsmay be resonance enhanced via porphyrin—* transitions. Upon l^ íitric oxide (NO) has been employed as a probe to detect the conformational change of the heme moiety in hemoglobin (Hb) when the quaternary structure is switched from the R to the T form (Rein et al., 1972; Cassoly, 1974; Taketa et al., 1975; Maxwell & Caughey, 1976; Perutz et al., 1976). Electron paramagnetic resonance (EPR) studies revealed that human nitrosylhemoglobin A (nitrosyl-HbA) in the R struc-f From the School of Chemistry, Georgia Instituteof Technology,