Resonance Raman spectra of myoglobins reconstituted with spirographis and isospirographis hemes and iron 2,4-diformylprotoporphyrin IX. Effect of formyl substitution at the heme periphery.
Resonance Raman spectra of myoglobins reconstituted with spirographis and isospirographis hemes and iron 2,4-diformylprotoporphyrin IX. Effect of formyl substitution at the heme periphery.
复制标题
用螺旋线虫和等螺旋线虫血红素以及 2,4-二甲酰基原卟啉 IX 铁重建的肌红蛋白的共振拉曼光谱。
DOI:
10.1021/bi00543a020
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发表时间:
1980
期刊:
影响因子:
2.9
通讯作者:
T. Kitagawa
中科院分区:
文献类型:
--
作者:
M. Tsubaki;K. Nagai;T. Kitagawa
Motonari Tsubaki, 1 Kiyoshi Nagai, and Teizo Kitagawa** abstract: Spirographis and isospirographis hemes and iron 2, 4-diformylprotoporphyrin IX were synthesized and their resonance Raman spectra were observed by incorporating them into sperm whale apomyoglobin (Mb) to protect them from photodegradation. The reconstituted Mb’s exhibited the formyl C= 0 stretching band around 1650-1670 cm" 1 both in reduced and in oxidized states and even in the ferric low-spin state, although the band is reported to be unobservable for cytochrome a of cytochrome oxidase. The C= 0 stretching frequencies clearly reflected nonequivalence of positions 2 and 4 of the porphyrin ring in the heme cavity of apoprotein. The Raman lines of native deoxy-Mb at 342 and 242 cm" 1 showed a frequency shift upon formyl substitution and were assigned to the porphyrin v8 and vl7 modes, respectively. The porphyrin CaCm stretching (10) and, though less sensitively, C „N stretching frequencies (v4) differed with the substituted pos-