期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:1972
卷号:69
期号:11
页码:3278-3282
DOI:10.1073/pnas.69.11.3278
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:The 13C-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.
关键词:magnetic interactions ; electron delocalization ; nuclear magnetic resonance ; electron spin resonance