Temperature dependence of CO ligation to LegHb and Mb: 0–80° C
Yazarlar (3)
| Makale Türü | Özgün Makale (Uluslararası alan indekslerindeki dergilerde yayınlanan tam makale) | ||
| Dergi Adı | Chemical physics letters | ||
| Makale Dili | – | Basım Tarihi | 12-1994 |
| Cilt / Sayı / Sayfa | 231 / 4 / 547–550 | DOI | – |
| Makale Linki | https://www.sciencedirect.com/science/article/pii/0009261494012954 | ||
| UAK Araştırma Alanları |
Dedektör Teknolojisi
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| Özet |
| The temperature dependence of the coordination of CO to two hemoproteins, myoglobin (Mb) and leghemoglobin (LegHb), has been studied by absorption spectroscopy. All spectral changes in the electronic and infrared ranges are fully reversible between 8 and 88°C and indicate a more linear orientation of the distal ligand with increasing temperature. The characteristic energy for the above spectral changes is around 200 cm−1 or identical to the Fe-Imidazole (Im) mode in hemoproteins. Our results are also compared with recent models for the dynamics of CO adsorbed at the surfaces of transition metals. Based on these surface models we suggest that our observed temperature dependences stem from thermal excitations of the Fe-Im vibration. This implies a so far undocumented mechanism by which the Fe-proximal bond influences the binding and energy dissipation at the active site of hemoproteins. |
| Anahtar Kelimeler |
