Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 407, Issue 2, Pages 196-201Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0003-9861(02)00471-X
Keywords
heme; porphyrin
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Funding
- NIDDK NIH HHS [R01 DK032303, DK32303, R56 DK032303] Funding Source: Medline
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The cDNA for p22HBP has been cloned from human and mouse, and the protein expressed, purified, and characterized. Both mouse and human proteins bind heme and porphyrins with micromolar K(d)s, are highly homologous, monomeric, and soluble, and have a cytoplasmic location. The proteins bind metalloporphyrins, free porphyrins, and N-methylprotoporphyrin with similar affinities, and mutations of a selected set of putative metal ligating residues did not have any significant effect on the measured K(d)s. That the presence or absence of metal in the porphyrin has no effect on the binding constants and the observation that the EPR signal for heme does not change upon binding to the protein strongly suggest that p22HBP is a generic tetrapyrrole-binding protein rather than a dedicated heme-binding protein. A role for p22HBP in cellular porphyrin metabolism is discussed. (C) 2002 Elsevier Science (USA). All rights reserved.
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