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Extended X-ray absorption fine structure studies of Zn/sub 2/Fe/sub 2/ hybrid hemoglobins: absence of heme bond length changes in half-ligated species

Journal Article · · Biochemistry; (United States)
OSTI ID:6868954
Metal hybrid hemoglobins, in which Zn(II) replaces Fe(II), have been structurally characterized by extended X-ray absorption structure (EAFS) studies. Since Zn and Fe have very different K absorption edge energies, the structures of the ligated (Fe) and unligated (Zn) sites could be examined independently within a single molecule that mimics an intermediate ligation state. The observed EXAFS spectra and associated structural parameters are compared among the ligand free (..cap alpha..Zn)/sub 2/(..beta..Zn)/sub 2/, half-ligated (..cap alpha..FeCO)/sub 2/(..beta..Zn)/sub 2/ and (..cap alpha..Zn)/sub 2/(..beta..FeCO)/sub 2/, and fully ligated (..cap alpha..FeCO)/sub 2/(..beta..FeCO)/sub 2/ systems.
Research Organization:
Univ. of Rochester, NY (USA)
OSTI ID:
6868954
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 25:13; ISSN BICHA
Country of Publication:
United States
Language:
English