Measurement of the protein-ligand bond energy of carboxymyoglobin by pulsed photoacoustic calorimetry |
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| Affiliation: | 1. Facultad de Ingeniería y Ciencias Agropecuarias, Universidad de las Américas, Av. Granados E12-41 y Colimes, Quito, Ecuador;2. Facultad de Ingeniería Sistemas, Escuela Politécnica Nacional, Ladrón de Guevara E11-253, Quito, Ecuador;3. I2A2 – ESTI Industriales, Universidad Politécnica de Madrid, C/ José Gutiérrez Abascal, 2, 28006 Madrid, Spain;4. Department of Economics, Texas A&M University, College Station, TX 77843, United States;1. Swinburne University of Technology Sarawak, Kuching, Sarawak 93350, Malaysia;2. Department of Architecture, Thiagarajar College of Engineering, Madurai TN-15, Tamilnadu, India;1. Department of Building Services Engineering, The Hong Kong Polytechnic University, Hong Kong, China;2. Faculty of Civil and Environmental Engineering, Universiti Tun Hussein Onn Malaysia, Parit Raja, 86400 Batu Pahat, Johor, Malaysia;3. Environmental Protection Department, The Hong Kong Special Administration Region Government, Hong Kong, China |
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| Abstract: | Pulsed photoacoustic spectroscopy has been used to study two horse heart myoglobin derivatives, deoxymyoglobin and carboxymyoglobin, in the temperature range of 0–25° C. The myoglobin-CO bond energy has been measured to be 13.4±0.5 kcal/mole. The volume change associated with the photodissociation of carboxymyoglobin into deoxymyoglobin and CO has also been observed. |
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