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@ARTICLE{Ritacco:890178,
      author       = {Ritacco, Ida and Saltalamacchia, Andrea and Spinello,
                      Angelo and Ippoliti, Emiliano and Magistrato, Alessandra},
      title        = {{A}ll-{A}tom {S}imulations {D}isclose {H}ow {C}ytochrome
                      {R}eductase {R}eshapes the {S}ubstrate {A}ccess/{E}gress
                      {R}outes of {I}ts {P}artner {CYP}450s},
      journal      = {The journal of physical chemistry letters},
      volume       = {11},
      number       = {4},
      issn         = {1948-7185},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2021-00767},
      pages        = {1189 - 1193},
      year         = {2020},
      abstract     = {Cytochromes P450 enzymes (CYP450s) promote the oxidative
                      metabolism of a variety of substrates via the electrons
                      supplied by the cytochrome P450 reductase (CPR) and upon
                      formation of a CPR/CYP450 adduct. In spite of the pivotal
                      regulatory importance of this process, the impact of CPR
                      binding on the functional properties of its partner CYP450
                      remains elusive. By performing multiple microsecond-long
                      all-atom molecular dynamics simulations of a 520 000-atom
                      model of a CPR/CYP450 adduct embedded in a membrane mimic,
                      we disclose the molecular terms for their interactions,
                      considering the aromatase (HA) enzyme as a proxy of the
                      CYP450 family. Our study strikingly unveils that CPR binding
                      alters HA’s functional motions, bolstering a change in the
                      shape and type of the channels traveled by
                      substrates/products during their access/egress to/from the
                      enzyme’s active site. Our outcomes unprecedentedly
                      contribute to extricate the many entangled facets of the
                      CYP450 metabolon, redrafting its intricate panorama from an
                      atomic-level perspective.},
      cin          = {IAS-5 / INM-9 / JARA-HPC},
      ddc          = {530},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      $I:(DE-82)080012_20140620$},
      pnm          = {899 - ohne Topic (POF3-899) / Post-Transcriptional
                      regulation mechanism of Human Aromatase investigated by
                      molecular simulations $(jias5a_20190501)$},
      pid          = {G:(DE-HGF)POF3-899 / $G:(DE-Juel1)jias5a_20190501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {31986051},
      UT           = {WOS:000515424300001},
      doi          = {10.1021/acs.jpclett.9b03798},
      url          = {https://juser.fz-juelich.de/record/890178},
}