| Literature DB >> 21875066 |
Omer Kabil1, Colin L Weeks, Sebastián Carballal, Carmen Gherasim, Beatriz Alvarez, Thomas G Spiro, Ruma Banerjee.
Abstract
Human CBS is a PLP-dependent enzyme that clears homocysteine, gates the flow of sulfur into glutathione, and contributes to the biogenesis of H(2)S. The presence of a heme cofactor in CBS is enigmatic, and its conversion from the ferric- to ferrous-CO state inhibits enzyme activity. The low heme redox potential (-350 mV) has raised questions about the feasibility of the ferrous-CO state forming under physiological conditions. Herein, we provide the first evidence of reversible inhibition of CBS by CO in the presence of a human flavoprotein and NADPH. These data provide a mechanism for cross talk between two gas-signaling systems, CO and H(2)S, via heme-mediated allosteric regulation of CBS.Entities:
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Year: 2011 PMID: 21875066 PMCID: PMC3183264 DOI: 10.1021/bi201270q
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162