Abstract
Heme degradation plays important biological roles, ranging from generating light-absorbing compounds in plants to facilitating iron homeostasis in mammals. The X-ray crystal structure of human heme oxygenase-1, which instigates the degradation process, reveals insights into the enzymatic mechanism of this important process.
References
Schuller, D.J., Wilks, A., Ortiz de Montellano, P.R. & Poulos, T.L. Nature Struct. Biol. 6, 860–867 (1999).
Tenhunen, R., Marver, H. S. & Schmid, R. J. Biol. Chem. 244, 6388– 6394 (1969).
Brown, S. B. & King, R. F. G. J. Biochem. J. 170 , 297–311 (1978).
Beale, S. I. In The biosynthesis of tetrapyrrole pigments. (ed. Chadwick, D. J. & Ackrill, K.) 156–171 (John Wiley & Sons, Chichester, UK; 1994).
Dore, S. et al. Proc. Natl. Acad. Sci USA 96, 2445– 2450 (1999).
Verma, A. et al. Science 259, 381–384 (1993).
Schmitt, M.P. J. Bacteriol. 179, 838–845 (1997).
Wilks. A. & Schmitt, M.P. J. Biol. Chem. 273, 837–841 (1998).
Poss, K.D. & Tonegawa, S. Proc. Natl. Acad. Sci. USA 94, 10919–10924 (1997).
Poss, K.D. & Tonegawa, S. Proc. Natl. Acad. Sci. USA 94, 10925–10930 (1997).
Wilks, A., Black, S.M., Miller, W.L. & Ortiz de Montellano, P.R. Biochemistry 34, 4421–4427 (1995).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Beale, S., Yeh, J. Deconstructing heme. Nat Struct Mol Biol 6, 903–905 (1999). https://doi.org/10.1038/13264
Issue Date:
DOI: https://doi.org/10.1038/13264
- Springer Nature America, Inc.
This article is cited by
-
Tyrosine oxidation in heme oxygenase: examination of long-range proton-coupled electron transfer
JBIC Journal of Biological Inorganic Chemistry (2014)