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/sup 31/P NMR probes of sipunculan erythrocytes containing the O/sub 2/-carying protein hemerythrin

Journal Article · · Biochemistry; (United States)
OSTI ID:6956125
Reported are the first examinations by /sup 31/P NMR of erythrocytes containing the non-heme iron O/sub 2/ carrying protein hemerythrin (Hr). Intact coelomic erythrocytes from the sipunculids Phascolopsis gouldii and Themiste zostericola were shown by /sup 31/P NMR to contain O-phosphorylethanolamine and 2-amino-ethylphosphonate as the major soluble phosphorus metabolites. This combination of major metabolites appears to be unique to sipunculan erythrocytes. Nucleoside triphosphates and mannose 1-phosphate were present in lower concentrations. The concentration of O-phosphorylethanolamine within P. gouldii erythrocytes was established to be > 20 mM. T. zostericola erythrocytes contained relatively high levels of 2-amino-ethylphosphonate and lower levels of O-phosphorylethanolamine compared with those of P. gouldii. For P. gouldii and T. zostericola the intracellular pHs were determined to be 7.2 +/- 0.1 and 7.1 +/- 0.1, respectively, in air-equilibrated erythrocytes, and 6.5 +/- 0.1 in anaerobic P. gouldii erythrocytes. O-Phosphorylethanolamine was found to bind weakly to P. gouldii metHr. This interaction is best characterized by either negative cooperativity or nonspecific binding. O-phosphorylethanolamine strongly inhibits azide binding to the iron site of P. gouldii metHr at pH 7.2. The rate of azide binding decreases by approx. 85-fold in the presence of 0.33 M O-phosphorylethanolamine. However, neither O-phosphorylethanolamine nor 2-aminoethylphosphonate at 0.33 M was found to have any significant effect on O/sub 2/ affinity of P. gouldii deoxyHr. Alternative functions for the two metabolites are suggested.
Research Organization:
Iowa State Univ., Ames (USA)
OSTI ID:
6956125
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:12; ISSN BICHA
Country of Publication:
United States
Language:
English