Direct observation of bis-sulfur ligation to the heme of bacterioferritin
Journal Article
·
· Journal of the American Chemical Society
- Stanford Univ., CA (United States)
- Brigham Young Univ., Provo, UT (United States)
- Exxon Research and Engineering Company, Annandale, NJ (United States)
X-ray absorption spectroscopy was used to examine the ligation of the heme of Azobacter vinelandii bacterioferritin scrupulously cleaned of non-heme iron. We find that the iron of the protoporphyrin IX of the protein has two axial sulfur ligands at 2.35 A, with four nitrogen ligands at 1.97 A. This result confirms the previous suggestion of Cheesman et al., on the basis of less direct spectroscopic techniques, that the heme of bacterioferritin is ligated by a pair of methionine ligands. To date, this mode of coordination is unknown in any other heme protein. 22 refs., 3 figs., 1 tab.
- OSTI ID:
- 41660
- Journal Information:
- Journal of the American Chemical Society, Journal Name: Journal of the American Chemical Society Journal Issue: 17 Vol. 115; ISSN JACSAT; ISSN 0002-7863
- Country of Publication:
- United States
- Language:
- English
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