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.
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 title = {Membrane environment drives cytochrome P450's spin transition and its interaction with cytochrome: B<inf>5</inf>},
 type = {article},
 year = {2017},
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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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