Modi S, Behere D V, Mitra S
Chemical Physics Group, Tata Institute of Fundamental Research, Colaba, Bombay, India.
Biochim Biophys Acta. 1994 Jan 11;1204(1):14-8. doi: 10.1016/0167-4838(94)90026-4.
The chemical modification of native horseradish peroxidase (HRP) has been carried out by esterification of the heme propionic group. 15N- and 1H-NMR studies on binding of thiocyanate ion to chemically modified HRP have been utilized to demonstrate the existence of salt bridge between the heme propionic acid and distal amino acid group. The catalyzed oxidation of thiocyanate by the native HRP, and the chemically modified HRP has also been studied at different pH, and the significance of the salt bridge discussed.
通过对血红素丙酸基团进行酯化反应，实现了对天然辣根过氧化物酶（HRP）的化学修饰。利用15N-和1H-NMR研究硫氰酸根离子与化学修饰的HRP的结合，以证明血红素丙酸与远端氨基酸基团之间存在盐桥。还研究了天然HRP和化学修饰的HRP在不同pH值下催化硫氰酸盐氧化的情况，并讨论了盐桥的意义。
