FTIR investigation of the conformational properties of the cyanide bound horse metmyoglobin |
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| Affiliation: | 1. Faculty of Foundry Engineering, AGH University of Science and Technology, 30-059 Krakow, Poland;2. Academic Centre for Materials and Nanotechnology, AGH University of Science and Technology, 30-059 Krakow, Poland;3. Department of Chemistry, Hankuk University of Foreign Studies, Yongin, Kyunggi-Do 449-791, Republic of Korea;1. Dipartimento di Scienze Fisiche e Chimiche, Università dell’Aquila, Via Vetoio 2, 67100, Coppito, L’Aquila, Italy;2. Sorbonne Universities, UPMC, Laboratoire de Réactivité de Surface UMR CNRS 7197, Tour 43-53, 3rd floor, 4 Pl. Jussieu, 75005, Paris, France;3. Service de Bioénergétique, Biologie Structurale et Mécanismes (SB2SM) CEA, iBiTec-S, Biochimie Biophysique et Biologie Structurale (B3S), I2BC, UMR 9198, F-91191 Gif-sur-Yvette, France;1. Research Center of Ecological Science & Femtosecond Laser Technology, College of Foundation Science, Harbin University of Commerce, Harbin, 150028, China;2. School of Computer and Information Engineering, Harbin University of Commerce, Harbin, 150028, China;3. National Key Laboratory of Science and Technology on Tunable Laser, Harbin Insitute of Technology, Harbin, 150080, China;1. Uzhhorod National University, 46 Pidhirna Str., 88000, Uzhhorod, Ukraine;2. Vlokh Institute of Physical Optics, 23 Dragomanov Str., 79005, Lviv, Ukraine;3. Semiconductor Physics, Chemnitz University of Technology, D-09107, Chemnitz, Germany;4. Institute of Electron Physics, Ukr. Nat. Acad. Sci., 21 Universytetska Str., 88017, Uzhhorod, Ukraine |
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| Abstract: | The IR spectra of horse metmyoglobin ligated with the various isotopic forms of the cyanide ion at pH 7.4 display an asymmetric isotope-sensitive profile in the C–N stretching region. Replacement of the water solvent by D2O or reducing the pH to 5.5 downshift the center frequency of the profiles by ≈1 cm−1 indicating that the Fe–C–N is hydrogen bonded. The measured profiles did not conform to any of the known peak shapes indicating that they are the sum of a number of overlapping peaks. Several techniques have been used to determine the exact number of overlapping peaks such as peak fitting, peak shape analysis and spectral deconvolution. The results indicate that the profiles are the sum of five C–N stretching bands. The five bands were attributed to the existence of the C–N vibrators in the cavities of different Mb-CN conformational states. The variations in the C–N stretching frequency were interpreted in term of the variation in polar interactions between the bound cyanide ion and the surrounding protein in these states. |
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