Revisit of the Interactions between Hydrogen Sulfide and Heme Proteins

ISSN: 1872-3136 (Online)
ISSN: 2212-7968 (Print)


Volume 8, 3 Issues, 2014


Download PDF Flyer




Current Chemical Biology

Aims & ScopeAbstracted/Indexed in


Submit Abstracts Online Submit Manuscripts Online

Editor-in-Chief:
Atta-ur-Rahman, FRS
Honorary Life Fellow
Kings College
University of Cambridge
Cambridge
UK
Email: ccb@benthamscience.org

View Full Editorial Board

Subscribe Purchase Articles Order Reprints


Revisit of the Interactions between Hydrogen Sulfide and Heme Proteins

Author(s): Toru Shimizu

Affiliation: Department of Cell Biology, Shantou University Medical College, 22 Xinling Road, Shantou, Guangdong, China P.C. 515041.

Abstract

Important roles for hydrogen sulfide (H2S) in physiological and pathological function are emerging. H2S is the fourth signaling gas molecule, following O2, NO and CO, that has been shown to be important for intra- and intermolecular signal transduction. These gas molecules should bind to the heme iron complex and regulate numerous important physiological functions such as transcription, guanylate cyclase, and phosphodiesterase. However, involvement of heme proteins in H2S-regulated functions has not been critically considered. This paper is to sort out the complicated interactions of H2S with heme proteins and to help advance our understanding of the molecular mechanism of the interaction between H2S and heme proteins. Importantly, H2S interacts with the heme iron complex of myoglobin and hemoglobin in the presence of H2O2, forming sulfheme (sulfur-incorporated porphyrin) iron complex with markedly different physicochemical characters (such as oxygen binding affinity) in contrast to those of the normal heme iron complex. It is suggested that involvement of the heme proteins in H2S-regulated physiological and pathological functions, in particular under oxidative stress conditions, is much more crucial than generally thought.

Keywords: Heme protein, Hydrogen sulfide, Reactive oxygen species, Signal transduction, Sulfheme.

Purchase Online Rights and Permissions

  
  



Article Details

Volume: 7
Issue Number: 2
First Page: 207
Last Page: 212
Page Count: 6
DOI: 10.2174/2212796811307020012
Advertisement

Related Journals




Webmaster Contact: urooj@benthamscience.org Copyright © 2014 Bentham Science