Packer E L, Sternlicht H, Rabinowitz J C
Proc Natl Acad Sci U S A. 1972 Nov;69(11):3278-82. doi: 10.1073/pnas.69.11.3278.
The (13)C-resonances of the 2',6'-ring carbon atoms of both tyrosyl residues of Clostridium acidi-urici ferredoxin are shifted downfield in the oxidized and reduced protein relative to these resonance positions in free tyrosine. These results show that both tyrosyl residues in the oxidized and reduced protein are in magnetically equivalent environments, and suggest that both tyrosyl residues are close to the two iron-sulfur clusters in the reduced and oxidized proteins and that each cluster is equally accessible to one reducing electron.
尿酸梭菌铁氧化还原蛋白两个酪氨酰残基的2',6'-环碳原子的(13)C共振,相对于游离酪氨酸中的这些共振位置,在氧化和还原蛋白中均向低场移动。这些结果表明,氧化和还原蛋白中的两个酪氨酰残基处于磁等价环境,并表明两个酪氨酰残基在还原和氧化蛋白中均靠近两个铁硫簇,且每个簇对一个还原电子的可及性相同。