Spectroscopic probes of homotropic and heterotropic interactions of the hemocyanin active site
β Scribed by Yeong Tsyr Hwang; Edward I. Solomon; Leonard J. Andrews
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 245 KB
- Volume
- 79
- Category
- Article
- ISSN
- 0020-1693
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β¦ Synopsis
spectra of the newly formed [4Fe-4S] cluster [6] correspond to those obtained for the subsites of the FdR cluster (Fig. 1). The data show that the externally added iron occupies either one subsite or at most two structurally equivalent sites of the [4Fe-4S] cluster [6, 71. This isotopic labeling of specific cluster subsites allows us to study in considerable detail the hyperfine interactions of the [4Fe4S] core structures. Moreover, this technique will allow us to correlate spectra of subsites in different oxidation states. Application of this technique of isotopic labeling to individual clusters of enzymes with multiple clusters (e.g., hydrogenase) will greatly simplify the spectral assignments.
Acknowledgements.
We are indebted to our colleagues who have contributed to the work described here, Drs.
π SIMILAR VOLUMES
Hemoglobin (Hb) from Chelidonichthys kumu was studied by resonance Raman and electronic absorption spectroscopy in the iron(III) and iron(II) states and in the presence of and CO at various pH values. All forms showed O 2 the appearance of two m(CxC) stretching modes around 1620 and 1630 cm-1 in con