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Q34577168-1DE81B2C-2BFF-4DFB-A9DC-DFE2B9FFBAD1
Q34577168-1DE81B2C-2BFF-4DFB-A9DC-DFE2B9FFBAD1
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http://www.wikidata.org/entity/statement/Q34577168-1DE81B2C-2BFF-4DFB-A9DC-DFE2B9FFBAD1
Distinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles.
P2860
Q34577168-1DE81B2C-2BFF-4DFB-A9DC-DFE2B9FFBAD1
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34577168-1DE81B2C-2BFF-4DFB-A9DC-DFE2B9FFBAD1
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wasDerivedFrom
0b814116dc41a13ce3db8fa63c59becb2ca315fe
P2860
Gating mechanisms for biological electron transfer: integrating structure with biophysics reveals the nature of redox control in cytochrome P450 reductase and copper-dependent nitrite reductase.