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Lei, Haotian, Bowler, Bruce E. (2019) Naturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity. The Journal of Physical Chemistry B, 123 (42). 8939-8953 doi:10.1021/acs.jpcb.9b05869

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Reference TypeJournal (article/letter/editorial)
TitleNaturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity
JournalThe Journal of Physical Chemistry B
AuthorsLei, HaotianAuthor
Bowler, Bruce E.Author
Year2019 (October 24)Volume123
Issue42
PublisherAmerican Chemical Society (ACS)
DOIdoi:10.1021/acs.jpcb.9b05869Search in ResearchGate
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Mindat Ref. ID3891325Long-form Identifiermindat:1:5:3891325:1
GUID0
Full ReferenceLei, Haotian, Bowler, Bruce E. (2019) Naturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity. The Journal of Physical Chemistry B, 123 (42). 8939-8953 doi:10.1021/acs.jpcb.9b05869
Plain TextLei, Haotian, Bowler, Bruce E. (2019) Naturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity. The Journal of Physical Chemistry B, 123 (42). 8939-8953 doi:10.1021/acs.jpcb.9b05869
In(2019, October) The Journal of Physical Chemistry B Vol. 123 (42) American Chemical Society (ACS)

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Lei, Haotian, Kelly, Allison D., Bowler, Bruce E. (2022) Alkaline State of the Domain-Swapped Dimer of Human Cytochrome c: A Conformational Switch for Apoptotic Peroxidase Activity. Journal of the American Chemical Society, 144 (46) 21184-21195 doi:10.1021/jacs.2c08325
Tarpani, Luigi, Bellezza, Francesca, Sassi, Paola, Gambucci, Marta, Cipiciani, Antonio, Latterini, Loredana (2019) New Insights into the Effects of Surface Functionalization on the Peroxidase Activity of Cytochrome c Adsorbed on Silica Nanoparticles. The Journal of Physical Chemistry B, 123 (11). 2567-2575 doi:10.1021/acs.jpcb.8b11762
Elmer-Dixon, Margaret M., Hoody, John, Steele, Harmen B. B., Becht, Dustin C., Bowler, Bruce E. (2019) Cardiolipin Preferentially Partitions to the Inner Leaflet of Mixed Lipid Large Unilamellar Vesicles. The Journal of Physical Chemistry B, 123 (43). 9111-9122 doi:10.1021/acs.jpcb.9b07690
Godbole, Shubhada, Bowler, Bruce E. (1997) A histidine variant of yeast iso-1-cytochrome c that strongly affects the energetics of the denatured state. Journal of Molecular Biology, 268 (5). 816-821 doi:10.1006/jmbi.1997.0999
Jiang, Xiuyun, Futera, Zdenek, Blumberger, Jochen (2019) Ergodicity-Breaking in Thermal Biological Electron Transfer? Cytochrome C Revisited. The Journal of Physical Chemistry B, 123 (35). 7588-7598 doi:10.1021/acs.jpcb.9b05253
Martin, Daniel R., Dinpajooh, Mohammadhasan, Matyushov, Dmitry V. (2019) Polarizability of the Active Site in Enzymatic Catalysis: Cytochrome c. The Journal of Physical Chemistry B, 123 (50). 10691-10699 doi:10.1021/acs.jpcb.9b09236
Tofoleanu, Florentina, Yuan, Ye, Pickard, Frank C., Tywoniuk, Bartłomiej, Brooks, Bernard R., Buchete, Nicolae-Viorel (2018) Structural Modulation of Human Amylin Protofilaments by Naturally Occurring Mutations. The Journal of Physical Chemistry B, 122 (21). 5657-5665 doi:10.1021/acs.jpcb.7b12083
Pandiscia, Leah A., Schweitzer-Stenner, Reinhard (2015) Coexistence of Native-Like and Non-Native Cytochrome c on Anionic Liposomes with Different Cardiolipin Content. The Journal of Physical Chemistry B, 119 (40). 12846-12859 doi:10.1021/acs.jpcb.5b07328
Ru, Xuyan, Crane, Brian R., Zhang, Peng, Beratan, David N. (2021) Why Do Most Aromatics Fail to Support Hole Hopping in the Cytochrome c Peroxidase–Cytochrome c Complex?. The Journal of Physical Chemistry B, 125 (28) 7763-7773 doi:10.1021/acs.jpcb.1c05064
McClelland, L. J., Mou, T.-C., Jeakins-Cooley, M. E., Sprang, S. R., Bowler, B. E. (2014) Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity. Proceedings of the National Academy of Sciences, 111 (18) 6648-6653 doi:10.1073/pnas.1323828111
Sahoo, Dipak Kumar, Jena, Subhrakant, Tulsiyan, Kiran Devi, Dutta, Juhi, Chakrabarty, Suman, Biswal, Himansu S. (2019) Amino-Acid-Based Ionic Liquids for the Improvement in Stability and Activity of Cytochrome c: A Combined Experimental and Molecular Dynamics Study. The Journal of Physical Chemistry B, 123 (47). 10100-10109 doi:10.1021/acs.jpcb.9b09278
 
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