Resonance Raman spectra of deoxyhemoproteins. Heme structure in relation to dioxygen binding

A. Desbois , M. Lutz , R. Banerjee
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引用次数: 12

Abstract

The low-frequency regions of the resonance Raman spectra of deoxygenated ferrous forms of soybean leghemoglobin a, horse myoglobin, sperm whale myoglobin, Aplysia myoglobin, stripped normal human hemoglobin (T quaternary form) and of stripped human NESdesArg-hemoglobin (R quaternary form) are reported. Differences observed among these spectra show that the globins of these hemoproteins impose various heme structures. In particular, the variable frequencies of band II (210–224 cm−1) and of band Ib (121–163 cm−1) show that an increase in dioxygen affinity corresponds to a decrease in Fe-N(pyrrole) bond length.

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脱氧血红蛋白的共振拉曼光谱。血红素结构与二氧结合的关系
报道了脱氧亚铁形式的大豆豆血红蛋白a、马肌红蛋白、抹香鲸肌红蛋白、海兔肌红蛋白、剥离的正常人血红蛋白(T季型)和剥离的人nesdesarg血红蛋白(R季型)的共振拉曼光谱的低频区。在这些光谱中观察到的差异表明,这些血红蛋白的球蛋白施加不同的血红素结构。特别是,波段II (210 ~ 224 cm−1)和波段Ib (121 ~ 163 cm−1)的频率变化表明,双氧亲和性的增加对应于Fe-N(吡咯)键长的减少。
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Author index Errata Protamine interacts with the D-domains of fibrinogen Studies on the primary structures of the exocellular d-alanyl-d-alanine peptidases of Streptomyces strain R61 and Actinomadura strain R39 Resonance Raman spectra of deoxyhemoproteins. Heme structure in relation to dioxygen binding
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