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：1981
卷号：78
期号：7
页码：4138-4140
DOI：10.1073/pnas.78.7.4138
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Resonance Raman spectra were obtained for monomeric oxymyohemerythrin and for the azide, thiocyanate, cyanate, cyanide, and fluoride adducts of metmyohemerythrin. The internal ligand vibrations in these complexes appear at essentially the same frequencies as those in the corresponding complexes of octameric hemerythrin. Likewise the Fe--O frequencies in H216O do not depend on quaternary structure of the protein. The anionic adducts fall into two classes in regard to isotope exchange behavior in H218O. They also manifest a novel photochemical transformation from one class of exchange behavior to the other. It seems evident that the functional site in hemerythrin exists in at least two different conformational states and that irradiation can stimulate isotope exchange in the exchange-resistant form.
关键词：oxo bridge ; iron protein ; oxygen isotope exchange ; photochemical conversion
