期刊
BIOCHEMISTRY
卷 50, 期 39, 页码 8261-8263出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi201270q
关键词
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资金
- National Institutes of Health [HL58984, GM33576]
- CSIC (Univesidad de la Republica)
Human CBS is a PLP-dependent enzyme that clears homocysteine, gates the flow of sulfur into glutathione, and contributes to the biogenesis of H2S. 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 H2S, via heme-mediated allosteric regulation of CBS.
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