Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 400, Issue 4, Pages 489-492Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.08.068
Keywords
Sulfhemoglobin; Sulfmyoglobin; Hemoglobin I (HbI); Hydrogen sulfide (H2S); Hydrogen peroxide (H2O2); Histidine (His); Ferryl species
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Funding
- National Science Foundation [0843608]
- NIH-NIGMS/MBRS-SCORE 5 [S06GM008103-36]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0843608] Funding Source: National Science Foundation
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Several hemoglobins were explored by UV-Vis and resonance Raman spectroscopy to define sulfheme complex formation. Evaluation of these proteins upon the reaction with H2O2 or O-2 in the presence of H2S suggest: (a) the formation of the sulfheme derivate requires a HisE7 residue in the heme distal site with an adequate orientation to form an active ternary complex; (b) that the ternary complex intermediate involves the HisE7, the peroxo or ferryl species, and the H2S molecule. This moiety precedes and triggers the sulfheme formation. (C) 2010 Elsevier Inc. All rights reserved.
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