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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jcsc/107/04/0497-0503

    • Keywords

       

      Hemeproteins; circular dichroism; alkaline transition; cytochrome c; horseradish peroxidase

    • 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.

    • Author Affiliations

       

      Tapan K Das1 Shyamalava Mazumdar1 Samaresh Mitra1

      1. Chemical Physics Group, Tata Institute of Fundamental Research, Homi Bhabha Road, Navynagar, Bombay - 400005, India

    • Dates

       
      Published
      August 1995

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