Journal article
Protein Dynamics in an Intermediate State of Myoglobin: Optical Absorption, Resonance Raman Spectroscopy, and X-Ray Structure Analysis
Biophysical journal, v 78(4), pp 2081-2092
2000
PMID: 10733986
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
A metastable state of myoglobin is produced by reduction of metmyoglobin at low temperatures. This is done either by irradiation with x-rays at 80
K or by electron transfer from photoexcited tris(2,2′-bipyridine)-ruthenium(II) at 20
K. At temperatures above 150
K, the conformational transition toward the equilibrium deoxymyoglobin is observed. X-ray crystallography, Raman spectroscopy, and temperature-dependent optical absorption spectroscopy show that the metastable state has a six-ligated iron low-spin center. The x-ray structure at 115K proves the similarity of the metastable state with metmyoglobin. The Raman spectra yield the high-frequency vibronic modes and give additional information about the distortion of the heme. Analysis of the temperature dependence of the line shape of the Soret band reveals that a relaxation within the metastable state starts at ∼120
K. Parameters representative of static properties of the intermediate state are close to those of CO-ligated myoglobin, while parameters representative of dynamics are close to deoxymyoglobin. Thus within the metastable state the relaxation to the equilibrium is initiated by changes in the dynamic properties of the active site.
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Details
- Title
- Protein Dynamics in an Intermediate State of Myoglobin: Optical Absorption, Resonance Raman Spectroscopy, and X-Ray Structure Analysis
- Creators
- Niklas Engler - Technical University of MunichAndreas Ostermann - Technical University of MunichAlexandra Gassmann - Technical University of MunichDon C. Lamb - Technical University of MunichValeri E. Prusakov - Russian Academy of SciencesJoachim Schott - University of BremenReinhard Schweitzer-Stenner - University of BremenFritz G. Parak - Technical University of Munich
- Publication Details
- Biophysical journal, v 78(4), pp 2081-2092
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:000086349500039
- Scopus ID
- 2-s2.0-0034028925
- Other Identifier
- 991019196815604721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biophysics