CO cage recombination in hemoglobin: Picosecond photolysis and nanosecond observation |
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| Affiliation: | 1. Laboratoire de Biologie Physico-Chimique, Université de Paris VII, Tour 42-43, 2, Place Jussieu, 75251 Paris, France;2. Institut Curie, 91405 Orsay, France;1. Department of Chemistry, Oklahoma State University, Stillwater, Oklahoma, USA;2. Department of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, Greenville, North Carolina, USA;3. Department of Chemistry, Mississippi State University, Mississippi State, Mississippi, USA;4. Department of Biochemistry, University of Missouri, Columbia, Missouri, USA;5. Department of Hematologic Malignancies and Cellular Therapeutics, The University of Kansas Medical Center, Kansas City, Kansas, USA;6. Department of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, Kansas, USA;1. Key Laboratory of Applied Surface and Colloid Chemistry, Ministry of Education, Shaanxi Key Laboratory for Advanced Energy Devices, Shaanxi Engineering Lab for Advanced Energy Technology, School of Materials Science & Engineering, Shaanxi Normal University, Xi''an 710119, P.R. China;2. Dalian National Laboratory for Clean Energy, iChEM, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, P.R. China;1. Institut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS, 71 Avenue des Martyrs, 38000 Grenoble, France;2. Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104 Freiburg, Germany;3. Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany;4. Structural Biology and NMR Laboratory, the Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark;5. Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany;6. European Molecular Biology Laboratory, 38042 Grenoble, France;7. BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany;1. Department of Materials Science and Engineering, Stanford University, Stanford, CA 94305, USA;2. Biophysics Program, School of Medicine, Stanford University, Stanford, CA 94305, USA;3. Department of Bioengineering, Stanford University, Stanford, CA 94305, USA;4. Department of Applied Physics, Stanford University, Stanford, CA 94305, USA;5. Division of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA;6. Stanford Institute for Materials and Energy Sciences, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA;1. College of Chemistry and Chemical Engineering, Shanghai University of Engineering Science, 333 Longteng Road, Shanghai 201620, China;2. School of Materials Science and Engineering, Shanghai University, 99 Shangda Road, Shanghai 200444, China;3. School of Physics and Materials Science, Guangzhou University, Guangzhou 510006, China;4. School of Materials Science and Engineering, Guilin University of Electronic Technology, Guilin 541004, China;1. I-Form Centre, School of Mechanical & Materials Engineering, University College Dublin, Belfield Dublin 4, Ireland;2. Croom Medical, Croom Enterprise Centre, Kilmallock Road, Croom, Co. Limerick, Ireland |
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| Abstract: | Carboxy hemoglobin in aqueous solution was photodissociated by laser pulses of 30 ps at 532 nm. Kinetic studies show that only upon complete photodissociation can the pure CO geminate binding process be revealed. The protein region of the iron cage, where the geminate ligand diffuses before reaching the heme, is smaller than a single subunit and larger than the heme pocket. |
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