@article{
 title = {Membrane environment drives cytochrome P450's spin transition and its interaction with cytochrome: B<inf>5</inf>},
 type = {article},
 year = {2017},
 identifiers = {[object Object]},
 volume = {53},
 id = {ee82c3d0-35a4-3e8b-b4e6-81c7a0722426},
 created = {2017-12-09T03:48:33.934Z},
 file_attached = {false},
 profile_id = {19ac30c5-f77a-3ba0-b82a-d16dd951269b},
 last_modified = {2017-12-15T23:56:33.724Z},
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 abstract = {© 2017 The Royal Society of Chemistry. Heme's spin-multiplicity is key in determining the enzymatic function of cytochrome P450 (cytP450). The origin of the low-spin state in ferric P450 is still under debate. Here, we report the first experimental demonstration of P450's membrane interaction altering its spin equilibrium which is accompanied by a stronger affinity for cytochrome b 5 . These results highlight the importance of lipid membrane for the function of P450.},
 bibtype = {article},
 author = {Ravula, T. and Barnaba, C. and Mahajan, M. and Anantharamaiah, G.M. and Im, S.-C. and Waskell, L. and Ramamoorthy, A.},
 journal = {Chemical Communications},
 number = {95}
}

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