Ondrias M R, Findsen E W, Gaul D F, Knaff D B
Biochim Biophys Acta. 1984 Jul 17;788(1):87-97. doi: 10.1016/0167-4838(84)90300-5.
Resonance Raman spectroscopy was employed to characterize the local heme environment of a high-spin, ligand-binding heme protein from Chromatium vinosum (Chromatium high-spin hemoprotein). High-frequency spectra obtained with both B- and Q-band excitation were found to resemble qualitatively those of deoxyhemoglobin (HbA). Differences between HbA and Chromatium high-spin hemoprotein spectra can be assigned to either the effects of a covalent linkage of the heme vinyls to the protein matrix or alterations in the heme-proximal ligand bonding interaction. Both kinematic and electronic effects were evident. The behavior of heme core-size sensitive modes and low-frequency modes in Chromatium high-spin hemoprotein may be an indication of distortions in the heme geometry of Chromatium high-spin hemoprotein relative to HbA. The effects of covalent bonding of the heme peripheral vinyls upon the vibrational, electronic, and geometric characteristics of the heme active site in Chromatium high-spin hemoprotein are discussed.
共振拉曼光谱法被用于表征来自嗜硫红假单胞菌（嗜硫红假单胞菌高自旋血红蛋白）的高自旋、配体结合血红蛋白的局部血红素环境。发现用B带和Q带激发获得的高频光谱在质量上类似于脱氧血红蛋白（HbA）的光谱。HbA和嗜硫红假单胞菌高自旋血红蛋白光谱之间的差异可归因于血红素乙烯基与蛋白质基质的共价连接效应或血红素近端配体键合相互作用的改变。运动学和电子效应均很明显。嗜硫红假单胞菌高自旋血红蛋白中血红素核心尺寸敏感模式和低频模式的行为可能表明嗜硫红假单胞菌高自旋血红蛋白相对于HbA的血红素几何结构存在扭曲。讨论了血红素外围乙烯基的共价键对嗜硫红假单胞菌高自旋血红蛋白中血红素活性位点的振动、电子和几何特征的影响。
