Membrane environment drives cytochrome P450's spin transition and its interaction with cytochrome: B<inf>5</inf>. Ravula, T., Barnaba, C., Mahajan, M., Anantharamaiah, G., Im, S., Waskell, L., & Ramamoorthy, A. Chemical Communications, 2017. abstract bibtex © 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.
@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},
read = {false},
starred = {false},
authored = {true},
confirmed = {false},
hidden = {false},
private_publication = {false},
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}
}
Downloads: 0
{"_id":"Qx2qZFjcpM4N8Kf79","bibbaseid":"ravula-barnaba-mahajan-anantharamaiah-im-waskell-ramamoorthy-membraneenvironmentdrivescytochromep450sspintransitionanditsinteractionwithcytochromebinf5inf-2017","downloads":0,"creationDate":"2017-12-10T06:09:36.266Z","title":"Membrane environment drives cytochrome P450's spin transition and its interaction with cytochrome: B<inf>5</inf>","author_short":["Ravula, T.","Barnaba, C.","Mahajan, M.","Anantharamaiah, G.","Im, S.","Waskell, L.","Ramamoorthy, A."],"year":2017,"bibtype":"article","biburl":null,"bibdata":{"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","read":false,"starred":false,"authored":"true","confirmed":false,"hidden":false,"private_publication":false,"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","bibtex":"@article{\n title = {Membrane environment drives cytochrome P450's spin transition and its interaction with cytochrome: B<inf>5</inf>},\n type = {article},\n year = {2017},\n identifiers = {[object Object]},\n volume = {53},\n id = {ee82c3d0-35a4-3e8b-b4e6-81c7a0722426},\n created = {2017-12-09T03:48:33.934Z},\n file_attached = {false},\n profile_id = {19ac30c5-f77a-3ba0-b82a-d16dd951269b},\n last_modified = {2017-12-15T23:56:33.724Z},\n read = {false},\n starred = {false},\n authored = {true},\n confirmed = {false},\n hidden = {false},\n private_publication = {false},\n 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.},\n bibtype = {article},\n author = {Ravula, T. and Barnaba, C. and Mahajan, M. and Anantharamaiah, G.M. and Im, S.-C. and Waskell, L. and Ramamoorthy, A.},\n journal = {Chemical Communications},\n number = {95}\n}","author_short":["Ravula, T.","Barnaba, C.","Mahajan, M.","Anantharamaiah, G.","Im, S.","Waskell, L.","Ramamoorthy, A."],"bibbaseid":"ravula-barnaba-mahajan-anantharamaiah-im-waskell-ramamoorthy-membraneenvironmentdrivescytochromep450sspintransitionanditsinteractionwithcytochromebinf5inf-2017","role":"author","urls":{},"downloads":0},"search_terms":["membrane","environment","drives","cytochrome","p450","spin","transition","interaction","cytochrome","inf","inf","ravula","barnaba","mahajan","anantharamaiah","im","waskell","ramamoorthy"],"keywords":[],"authorIDs":[]}