Structural studies of the hemocyanin active site. 1. Extended x-ray absorption fine structure (EXAFS) analysis
- 1 June 1980
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 102 (12) , 4210-4216
- https://doi.org/10.1021/ja00532a037
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Spectroscopic studies of ligand perturbation effects on the half oxidized active site of busycon canaliculatum hemocyaninBiochemical and Biophysical Research Communications, 1978
- Crystals of a functional 70,000 molecular weight subunit of hemocyanin from Limulus polyphemusJournal of Molecular Biology, 1977
- Biological analogs. Nature of the binding sites of copper-containing proteinsJournal of the American Chemical Society, 1977
- X-ray absorption studies of halide binding to carbonic anhydrase.Proceedings of the National Academy of Sciences, 1977
- Resonance Raman spectroscopy with unsymmetrically isotopic ligands. Differentiation of possible structures of hemerythrin complexesJournal of the American Chemical Society, 1976
- A resonance Raman study of the copper protein, hemocyanin. New evidence for the structure of the oxygen-binding siteJournal of the American Chemical Society, 1976
- Observations and interpretation of x-ray absorption edges in iron compounds and proteins.Proceedings of the National Academy of Sciences, 1976
- Structure-function relations in hemoglobin as determined by x-ray absorption spectroscopy.Proceedings of the National Academy of Sciences, 1976
- The effect of photooxidation and histidine reagents on Murex trunculus haemocyaninBiochimica et Biophysica Acta (BBA) - Protein Structure, 1968
- Copper Proteins and OxygenThe Journal of general physiology, 1965