X-ray absorption spectroscopy of hemocyanin and hemerythrin
The oxygen binding site of hemocyanin has two copper atoms coordinated to the side chains from the polypeptide chain. Copper extended x-ray absorption fine structure (EXAFS) and absorption edges of the protein were studied. Comparison of EXAFS from three molluscan oxyhemocyanins (Megathura crenulata, the ..cap alpha../sub c/ and ..beta../sub c/ of Helix pomatia) indicates that the structure of the binuclear copper sites is very similar in the three proteins. Four different forms (oxy, deoxy, dimer, and half-apo) of hemocyanin from M. crenulata were selected for a detailed study. A structural model of the oxygen binding site is proposed based on the EXAFS results. The oxygen binding site in hemerythrin contains two iron atoms coordinated to the side chains from the polypeptide chain. Iron EXAFS and absorption edges from Phascolopsis gouldii hemerythrin were studied. Five different forms (oxy, deoxy, aquomet, hydroxomet, and azidomet) of the protein were selected for this study. A structural model of the oxygen binding site in hemerythrin is proposed.
- Research Organization:
- Stanford Univ., CA (USA). Stanford Synchrotron Radiation Lab.
- DOE Contract Number:
- AC03-76SF00515
- OSTI ID:
- 6917611
- Report Number(s):
- SSRL-84/02; ON: DE84010930
- Resource Relation:
- Other Information: Portions are illegible in microfiche products. Thesis
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
COPPER CHLORIDES
X-RAY SPECTROSCOPY
COPPER COMPLEXES
COPPER OXIDES
COPPER SULFIDES
HEMOCYANIN
FOURIER TRANSFORMATION
IMIDAZOLES
INVERTEBRATES
ANIMALS
AZOLES
CHALCOGENIDES
CHLORIDES
CHLORINE COMPOUNDS
COMPLEXES
COPPER COMPOUNDS
COPPER HALIDES
HALIDES
HALOGEN COMPOUNDS
HETEROCYCLIC COMPOUNDS
INTEGRAL TRANSFORMATIONS
METALLOPROTEINS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXIDES
OXYGEN COMPOUNDS
PROTEINS
SPECTROSCOPY
SULFIDES
SULFUR COMPOUNDS
TRANSFORMATIONS
TRANSITION ELEMENT COMPLEXES
TRANSITION ELEMENT COMPOUNDS
550200* - Biochemistry