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：1982
卷号：79
期号：5
页码：1511-1514
DOI：10.1073/pnas.79.5.1511
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The iron-histidine stretching mode in deoxyhemoglobin displays a large change in frequency and width upon lowering the temperature from 300 to 10 K. The temperature dependence of the data indicates the presence of dynamic process. The dynamics of this mode in frozen hemoglobins can be qualitatively and quantitatively described as a vibrational dephasing via anharmonic coupling to other vibrations of the heme-imidazole system. the effect that occur at the melting transition in the low frequency modes cannot be quantitatively addressed at this point but may be indicative of the introduction of additional degrees of freedom predicated on protein influences that reflect differences in protein quaternary structure.
