XAFS study of CO binding to denatured cytochrome c
β Scribed by Y. Zhang; E.A. Stern
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 117 KB
- Volume
- 208-209
- Category
- Article
- ISSN
- 0921-4526
No coin nor oath required. For personal study only.
β¦ Synopsis
X-ray absorption fine structure (XAFS) measurements were made of native cytochrome c, denatured cytochrome c and its CO-bonded form. Our results show that the local structure around the heme site in denatured ferrous cytochrome c is not significantly different from the one in native ferrous cytochrome c. Our results also indicate that when CO binds to denatured ferrous cytochrome c, CO takes place of the S ligand, possible unfolding the denatured ferrous cytochrome c further.
π SIMILAR VOLUMES
Novel devices for the spectroscopic and chromatographic analysis of the denaturation curves of the protein are described. A multidimensional spectroscopic measuring system makes it possible to carry out simultaneous and continuous acquisition of a set of data of different spectroscopic dimensions at