摘要
Detailed circular dichroism(CD) and Fourier transform infrared(FTIR) studies have been carried out to monitor thermal unfolding of horseradish peroxidase isoenzyme C(HRP) inhibited by CN -(HRP CN). The results suggest that HRP CN is quite different from native HRP with different spin states of Fe of heme and different coordinated states. Cyanide becomes the sixth ligand of Fe(Ⅲ) of heme and the hydrogen binding network is destroyed partly at the same time, which cause the drastic decrease of thermal stability of HRP. The FTIR and Soret CD spectra analysis demonstrate that during the heating process there is an intermediate state(I) which has both partly destroyed secondary and tertiary structures of native HRP, then it is the appearance of protein aggregation state(A) after fully unfolding. The unfolding pathway thus can be shown as follows: IIUA.
Detailed circular dichroism(CD) and Fourier transform infrared(FTIR) studies have been carried out to monitor thermal unfolding of horseradish peroxidase isoenzyme C(HRP) inhibited by CN -(HRP CN). The results suggest that HRP CN is quite different from native HRP with different spin states of Fe of heme and different coordinated states. Cyanide becomes the sixth ligand of Fe(Ⅲ) of heme and the hydrogen binding network is destroyed partly at the same time, which cause the drastic decrease of thermal stability of HRP. The FTIR and Soret CD spectra analysis demonstrate that during the heating process there is an intermediate state(I) which has both partly destroyed secondary and tertiary structures of native HRP, then it is the appearance of protein aggregation state(A) after fully unfolding. The unfolding pathway thus can be shown as follows: IIUA.
出处
《高等学校化学学报》
SCIE
EI
CAS
CSCD
北大核心
2001年第7期1131-1133,共3页
Chemical Journal of Chinese Universities
基金
国家自然科学基金 (批准号 :2 9835 12 0
2 9875 0 2 8)
