Encyclopedia of Biophysics

2013 Edition
| Editors: Gordon C. K. Roberts

Hemes

  • Brian R. GibneyEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-3-642-16712-6_43

Synonyms

Definition

Heme, the ferrous iron complex of protoporphyrin IX, is a common prosthetic group in proteins including the electron transfer  cytochromes, the respiratory complexes, and the oxygen carrier hemoglobin.

Basic Characteristics

Introduction

Iron porphyrins, including iron (protoporphyrin IX) or heme b, are one of the most versatile and visible classes of redox cofactors utilized in biochemistry and biophysics. Naturally occurring from archaebacteria to mammals, heme proteins carry out diverse biochemical tasks such as electron transfer, substrate oxidation, metal-ion storage, ligand sensing/transport, and gene regulation. Thus, heme proteins are critical components in numerous biological processes including hormone and steroid biosynthesis, drug metabolism, aerobic respiration, and even programmed cell death. The dysfunction of natural heme proteins leads to a myriad of human diseases including...

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References

  1. Antonini E, Brunori M. Hemoglobin and myoglobin in their reactions with ligands. Amsterdam: North-Holland; 1971.Google Scholar
  2. Dolphin D. The porphyrins. New York: Academic; 1978.Google Scholar
  3. Dunford HB. Heme peroxidases. New York: Wiley; 1999.Google Scholar
  4. Ortiz de Montellano PR. Cytochrome P450: structure, function, and mechanism. 2nd ed. New York: Plenum; 1995.Google Scholar
  5. Reedy CJ, Gibney BR. Heme protein assemblies. Chem Rev. 2004;104:589–604.Google Scholar
  6. Scott RA, Mauk AG. Cytochrome c – a multidisciplinary approach. Sausalito: University Science; 1996.Google Scholar

Copyright information

© European Biophysical Societies' Association (EBSA) 2013

Authors and Affiliations

  1. 1.Department of ChemistryBrooklyn College – The City University of New YorkBrooklynUSA