Vinck Evi, Van Doorslaer Sabine, Dewilde Sylvia, Moens Luc
Department of Physics, University of Antwerp, B-2610 Antwerp, Belgium.
J Am Chem Soc. 2004 Apr 14;126(14):4516-7. doi: 10.1021/ja0383322.
Human neuroglobin (hNgb) and human cytoglobin (hCygb), two recently discovered members of the vertebrate globin family, are known to be able to form an intramolecular disulfide bridge. Using electron paramagnetic resonance (EPR), we show that formation of a disulfide bridge in ferric hNgb causes a considerable change in the heme pocket structure, whereas this is not so clear for ferric hCygb. The structural results can be related nicely to earlier histidine and dioxygen affinity studies of the ferrous proteins.
人类神经球蛋白（hNgb）和人类细胞球蛋白（hCygb）是脊椎动物球蛋白家族中最近发现的两个成员，已知它们能够形成分子内二硫键。利用电子顺磁共振（EPR），我们发现三价铁hNgb中二硫键的形成会导致血红素口袋结构发生显著变化，而对于三价铁hCygb来说，情况并非如此清晰。这些结构结果可以很好地与之前对亚铁蛋白的组氨酸和双氧亲和力研究联系起来。
