Structural and Functional Characterization of a Cytochrome P450 2B4 F429H Mutant with an Axial Thiolate–Histidine Hydrogen Bond

[Image: see text] The structural basis of the regulation of microsomal cytochrome P450 (P450) activity was investigated by mutating the highly conserved heme binding motif residue, Phe429, on the proximal side of cytochrome P450 2B4 to a histidine. Spectroscopic, pre-steady-state and steady-state ki...

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Hlavní autoři: Yang, Yuting, Zhang, Haoming, Usharani, Dandamudi, Bu, Weishu, Im, Sangchoul, Tarasev, Michael, Rwere, Freeborn, Pearl, Naw May, Meagher, Jennifer, Sun, Cuthbert, Stuckey, Jeanne, Shaik, Sason, Waskell, Lucy
Médium: Artigo
Jazyk:Inglês
Vydáno: American Chemical Society 2014
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC4131899/
https://ncbi.nlm.nih.gov/pubmed/25029089
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi5003794
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