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共振拉曼光谱证据表明,远端组氨酸质子化消除了肌红蛋白对一氧化碳垂直结合的空间位阻。

Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobin.

作者信息

Ramsden J, Spiro T G

机构信息

Department of Chemistry, Princeton University, New Jersey 08544-1009.

出版信息

Biochemistry. 1989 Apr 18;28(8):3125-8. doi: 10.1021/bi00434a001.

DOI:10.1021/bi00434a001
PMID:2545246
Abstract

The resonance Raman band assigned to Fe--CO stretching in the sperm whale myoglobin CO adduct shifts from 507 cm-1 at neutral pH to 488 cm-1 at low pH, in concert with a shift of the C-O stretching infrared band from 1947 to 1967 cm-1 (Fuchsman & Appleby, 1979), while the 575-cm-1 Fe-C-O bending RR band loses intensity. The pKa that characterizes these changes is approximately 4.4. The vibrational frequencies at low pH are well modeled by the protein-free CO, imidazole adduct of protoheme in a nonpolar solvent while those at high pH are modeled by the adduct of a heme with a covalent strap (Yu et al., 1983) which inhibits upright CO binding. It is inferred that the Fe-C-O unit changes from a tilted to an upright geometry when the distal histidine is protonated, because its side chain swings out of the heme pocket due to electrostatic repulsion with a nearby arginine residue. A different protonation step (pKa = 5.7), which has been shown to modulate the CO rebinding kinetics (Doster et al., 1982) as well as the optical spectrum (Fuchsman & Appleby, 1979), is suggested to involve a global structure change associated with protonation of histidine residues distant from the heme.

摘要

抹香鲸肌红蛋白一氧化碳加合物中归属于铁-羰基伸缩振动的共振拉曼带,在中性pH值下为507厘米-1,在低pH值下移至488厘米-1,同时碳-氧伸缩红外带从1947厘米-1移至1967厘米-1(富克斯曼和阿普尔比,1979年),而575厘米-1的铁-碳-氧弯曲共振拉曼带强度减弱。表征这些变化的pKa约为4.4。低pH值下的振动频率可以很好地由原血红素在非极性溶剂中的无蛋白一氧化碳、咪唑加合物模拟,而高pH值下的振动频率则由带有共价带的血红素加合物模拟(于等人,1983年),该共价带抑制一氧化碳垂直结合。据推断,当远端组氨酸质子化时,铁-碳-氧单元从倾斜构型变为垂直构型,因为其侧链由于与附近精氨酸残基的静电排斥而摆动出血红素口袋。另一个质子化步骤(pKa = 5.7),已被证明可调节一氧化碳再结合动力学(多斯特等人,1982年)以及光谱(富克斯曼和阿普尔比,1979年),有人认为这涉及与远离血红素的组氨酸残基质子化相关的整体结构变化。

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