Please use this identifier to cite or link to this item: http://hdl.handle.net/11717/3677
Title: Metal ion environment in reconstituted hemoglobins and myoglobins
Authors: Manoharan, P.T.
Issue Date: 1990
Publisher: Springer-Verlag
Citation: Proceedings of the Indian Academy of Sciences - Chemical Sciences, 102(3), 337-352
Abstract: Studies on reconstituted hemeproteins, viz, hemoglobin and myoglobin, with metal ions such as Co(II), Ni(II) and Cu(II), using a variety of spectroscopic techniques such as EPR, NMR, resonance Raman and optical, indicate three levels at which the metal ion coordinations are influenced by protein conformation. While in monomeric proteins the type of coordination, essentially a five-coordinate one, is determined by the protein conformation in the heme pocket, the sub-unit interactions in tetrameric proteins can produce a mixture of two types of coordination in individual proteins, one similar to that in monomeric proteins and the other a four-coordinate one with a possible weak axial coordination. As a result, tetrameric proteins with Ni(II) as the metal ion reveal the presence of differing spin states. Furthermore, it is proved that the effects on the proximal histidine associated with the R and T quaternary conformation influence the five-coordinated sites. Some results on hybrid hemoglobins as well as those from isolated chains are also reported. ? 1990 Indian Academy of Sciences.
URI: http://dx.doi.org/10.1007/BF02841947
http://hdl.handle.net/11717/3677
ISSN: 2534134
Appears in Collections:Articles

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.