期刊
BIOCHEMISTRY
卷 48, 期 29, 页码 7056-7071出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi900697c
关键词
-
资金
- NIH [HL-66147]
- NCIC [010200]
Nuclear receptors E75, which regulates development in Drosophila melanogaster, and Rev-erb beta, which regulates circadian rhythm in humans, bind heme within their ligand binding, domains (LBD). The heme-bound ligand binding domains of E75 and Rev-erb beta Were studied using electronic absorption, MCD, resonance Raman, and EPR spectroscopies. Both proteins undergo redox-dependent ligand switching and CO- and NO-induced ligand displacement. In the Fe(I 11) oxidation state, the nuclear receptor hemes are low spin and 6-coordinate with cysteine(thiolate) as one of the two axial heme ligands. The sixth ligand is a neutral donor, presumably histidine. When the heme is reduced to the Fe(l 1) oxidation state, the cysteine(thiolate) is replaced by a different neutral donor ligand, whose identity is not known, CO binds to the Fe(II) heme in both E75(LBD) and Rev-erb beta(LBD) opposite a sixth neutral ligand, plausibly the same histidine that served as the sixth ligand in the Fe(III) state. NO binds to the heme of both proteins; however, the NO-heme is 5-coordinate in E75 and 6-coordinate in Rev-erb beta. These nuclear receptors exhibit coordination characteristics that are similar to other known redox and Gas sensors, suggesting that E75 and Rev-erb beta may function in heme-, redox-, or gas-regulated control of cellular function.
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