Heme CD as a probe for monitoring local structural changes in hemeproteins: Alkaline transition in hemeproteins

Abstract

Structural change due to acid-alkaline transition in hemeproteins were monitored by circular dichroism measurements in the Soret region. It was observed that in cytochrome c and horseradish peroxidase, alkaline transition results in a large change in the heme CD due to significant conformational change in the heme cavity region. In metmyoglobin a simple protolytic mechanism associated with alkaline transition involves very small conformational changes. © 1995 Indian Academy of Sciences.