期刊
FEBS LETTERS
卷 593, 期 12, 页码 1351-1359出版社
WILEY
DOI: 10.1002/1873-3468.13436
关键词
enzymatic mechanism; NO reduction; non-heme iron; O-2 reduction
资金
- Swedish Research Council [2015-04512] Funding Source: Swedish Research Council
- Vetenskapsrådet [2015-04512] Funding Source: Medline
A key step of denitrification, the reduction of toxic nitric oxide to nitrous oxide, is catalysed by cytochrome c-dependent NO reductase (cNOR). cNOR contains four redox-active cofactors: three hemes and a nonheme iron (Fe-B). Heme b(3) and Fe-B constitute the active site, but the specific mechanism of NO-binding events and reduction is under debate. Here, we used a recently constructed, fully folded and hemylated cNOR variant that lacks Fe-B to investigate the role of Fe-B during catalysis. We show that in the Fe-B-less cNOR, binding of both NO and O-2 to heme b(3) still occurs but further reduction is impaired, although to a lesser degree for O-2 than for NO. Implications for the catalytic mechanisms of cNOR are discussed.
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