Przywarska-Boniecka H, Swirska H
J Inorg Biochem. 1980 Dec;13(4):283-96. doi: 10.1016/s0162-0134(00)80249-4.
Artificial hemoglobins have been prepared with Mn(III) and Zn(II) tetrasulfonated phthalocyanines in place of heme. Their structure and properties have been investigated by difference spectroscopy, CD, epr, electrophoresis, and molecular weight estimation. Spectrophotometric titration data indicate the ratio of the reagents in this process to be 1:1. The visible absorption spectra show the main peak at 625 nm for the manganese compound and 681 nm for the zinc one. It is evident from CD experiments that incorporation of MN(III)L into apohemoglobin increases helical content of the protein whereas that of Zn(II)L increases its unfolding due to the change of electronic configuration of Zn(II) ion on coordination with the protein. On the basis of spectroscopic and epr data, the formula of the manganese complex is suggested to be (O)Mn(IV)L-globin, whereas that of the zinc complex Zn(II)L-globin. Electrophoresis and molecular weight estimation indicate both complexes to be dimers. Manganese complex binds additional ligands as CN-, imidazole, CO, and NO. Spectroscopic and epr data indicate reduction of the manganese complex and formation of the NO adduct with probable formula (NO) + Mn(II)L-globin. Mechanism of this process is suggested. Both phthalocyanine globins are not able to combine reversibly with oxygen and cannot act as physiological oxygen carriers.
已经制备了用锰（III）和锌（II）四磺化酞菁代替血红素的人工血红蛋白。通过差示光谱、圆二色性（CD）、电子顺磁共振（epr）、电泳和分子量估计对它们的结构和性质进行了研究。分光光度滴定数据表明该过程中试剂的比例为1:1。可见吸收光谱显示锰化合物在625nm处有主峰，锌化合物在681nm处有主峰。从CD实验可以明显看出，将MN（III）L掺入脱辅基血红蛋白中会增加蛋白质的螺旋含量，而Zn（II）L的掺入则由于Zn（II）离子与蛋白质配位时电子构型的变化而增加其解折叠程度。根据光谱和epr数据，锰配合物的化学式被认为是（O）Mn（IV）L-球蛋白，而锌配合物的化学式是Zn（II）L-球蛋白。电泳和分子量估计表明两种配合物都是二聚体。锰配合物能结合额外的配体，如CN-、咪唑、CO和NO。光谱和epr数据表明锰配合物发生还原并形成可能化学式为（NO）+Mn（II）L-球蛋白的NO加合物。提出了该过程的机制。两种酞菁球蛋白都不能与氧可逆结合，也不能作为生理性氧载体。
