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Nitric oxide blocks cellular heme insertion into a broad range of heme proteins
S M WAHEED, A GHOSH, R CHAKRAVARTI, A BISWAS, M M HAQUE, , D J STUEHR
Published in ELSEVIER SCIENCE INC
2010
PMID: 20211245
Volume: 48
   
Issue: 11
Pages: 1548 - 1558
Abstract
Although the insertion of heme into proteins enables their function in bioenergetics, metabolism, and signaling, the mechanisms and regulation of this process are not fully understood. We developed a means to study cellular heme insertion into apo-protein targets over a 3-h period and then investigated how nitric oxide (NO) released from a chemical donor (NOC-18) might influence heme (protoporphyrin IX) insertion into seven targets that present a range of protein structures, heme ligation states, and functions (three NO synthases, two cytochrome P450's, catalase, and hemoglobin). NO blocked cellular heme insertion into all seven apo-protein targets. The inhibition occurred at relatively low (nM/min) fluxes of NO, was reversible, and did not involve changes in intracellular heme levels, activation of guanylate cyclase, or inhibition of mitochondrial ATP production. These aspects and the range of protein targets suggest that NO can act as a global inhibitor of heme insertion, possibly by inhibiting a common step in the process. © 2010 Elsevier Inc.
About the journal
JournalData powered by TypesetFree Radical Biology and Medicine
PublisherData powered by TypesetELSEVIER SCIENCE INC
ISSN0891-5849
Open AccessNo