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:1974
卷号:71
期号:11
页码:4546-4550
DOI:10.1073/pnas.71.11.4546
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:Data obtained by means of proton magnetic resonance spectroscopy indicate that specific association of FMN occurs with AMP in aqueous solution, because much weaker interaction is observed with FMN of either GMP or CMP. A comparison of FAD with a 1:1 mixture of FMN and AMP suggests that the flavin is involved in an intramolecular hydrogen bonding with the adenine moiety of FAD. The temperature dependence of chemical shifts would seem to indicate that the pyrophosphate linkage acts to reinforce stacking interactions as well as hydrogen bonding in the coenzyme. The linkage also limits the number of cyclic hydrogen bonding configurations, and a model is proposed to describe a fraction of unstacked FAD in aqueous solution. A parallel study was made of NAD+ and its analogues; in contrast to FAD, no clear evidence of cyclic hydrogen bonding was obtained with the pyridine coenzymes.
关键词:structure of FAD in aqueous solution ; 220 MHz proton magnetic resonance ; DPN+ and derivatives