Electron Spin Resonance Studies on Cobalt Carbonic Anhydrase-Substrate Complexes

Authors

Çigdem NUHOĞLU
Nazan DEMİR
Barbaros NALBANTOĞLU
Ö. İrfan KÜFREVİOĞLU
Y. Kemal YOĞURTÇU
Hasan ÖZDEMİR
Enise AYYILDIZ

Abstract

The native zinc atom of bovine erythrocyte carbonic anhydrase purified by affinity choromatography was removed by dialysis against pyridine 2,6-dicarboxylic acid. Cobalt carbonic anhydrase was prepared from the zinc-free apoenzyme. The binding conditions of CO_2 and p-nitrophenylacetate to cobalt carbonic anhydrase were investigated by electron spin resonance at different pH levels.

DOI

-

Keywords

Bovine carbonic anhydrase, ESR spectroscopy, substrate complexes.

First Page

134

Last Page

138

Recommended Citation

NUHOĞLU, Ç, DEMİR, N, NALBANTOĞLU, B, KÜFREVİOĞLU, Ö. İ, YOĞURTÇU, Y. K, ÖZDEMİR, H, & AYYILDIZ, E (1997). Electron Spin Resonance Studies on Cobalt Carbonic Anhydrase-Substrate Complexes. Turkish Journal of Chemistry 21 (2): 134-138. https://doi.org/-