Vuk-pavlović S, Benko B, Maricić S, Lahajnar G, Kuranova I P, Vainshtein B K
Int J Pept Protein Res. 1976;8(5):427-34. doi: 10.1111/j.1399-3011.1976.tb02522.x.
Using the solvent-protons' longitudinal magnetic relaxation rates (p.m.r.) for Lupinus luteus leghaemoglobin derivatives the accessibility of the haem has been evaluated by our "stereo-chemical p.m.r. titration" method with nonexchangeable protons of aliphatic lower alcohols in otherwise deuterated solutions. The haem in leghaemoglobin is more accessible and its protein environment more flexible compared with vertebrate haemoglobins. The correlation time in aquometleghaemglobin aqueous solution has been determined by measuring the frequency dispersion of the p.m.r. rates between 6.1 and 93 MHZ. Taking into account the measured value of tauc = (7.7 +/- 0.5 x 10(-10) s the iron-to-proton inter-spin distances have been calculated. The significance of these distances as well as the electronic g-factor anisotrophy for elucidation of fine structural details of the haem-environment are discussed.
利用羽扇豆血红蛋白衍生物中溶剂质子的纵向磁弛豫率（核磁共振），通过我们的“立体化学核磁共振滴定”方法，在其他方面为氘代溶液中，用脂肪族低级醇的不可交换质子评估了血红素的可及性。与脊椎动物血红蛋白相比，豆血红蛋白中的血红素更容易接近，其蛋白质环境更具灵活性。通过测量6.1至93兆赫兹之间核磁共振速率的频率色散，确定了水合高铁豆血红蛋白水溶液中的相关时间。考虑到测量值τc =（7.7±0.5×10⁻¹⁰秒），计算了铁与质子之间的自旋间距。讨论了这些距离以及电子g因子各向异性对于阐明血红素环境精细结构细节的意义。
