Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Kimberly Rizzolo"'
Autor:
Kimberly Rizzolo, Steven E. Cohen, Andrew C. Weitz, Madeline M. López Muñoz, Michael P. Hendrich, Catherine L. Drennan, Sean J. Elliott
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG
Externí odkaz:
https://doaj.org/article/43e89e2788134c44bc04e90574efd768
Autor:
Steven E. Cohen, Catherine L. Drennan, Andrew C. Weitz, Michael P. Hendrich, Sean Elliott, Kimberly Rizzolo
Publikováno v:
J Am Chem Soc
BthA is a diheme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generating a highly unusual Fe(IV)Fe(IV)=O oxidation state, known to be responsible for long-range oxidative chemistry in the enzyme MauG. Here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::268c0ef2e799e45188d81663fbeac15d
https://doi.org/10.1021/jacs.0c04023
https://doi.org/10.1021/jacs.0c04023
Publikováno v:
Biochemistry. 57:6416-6433
Cytochrome c peroxidases (bCcPs) are diheme enzymes required for the reduction of H2O2 to water in bacteria. There are two classes of bCcPs: one is active in the diferric form (constitutively active), and the other requires the reduction of the high-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dc7a4b21a9b8a81284b5d849266a4780
https://doi.org/10.1021/acs.biochem.8b00732
https://doi.org/10.1021/acs.biochem.8b00732
Autor:
Steven E. Cohen, Catherine L. Drennan, Madeline M. López Muñoz, Andrew C. Weitz, Sean Elliott, Michael P. Hendrich, Kimberly Rizzolo
Publikováno v:
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (H2O2) reduction to post-translational modifications. By implementing a sequence similarity network (SSN) of the bCCP_MauG superfamily, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a33ed2a3060de56bdcfc0858acfd7f16
https://doi.org/10.1038/s41467-019-09020-4
https://doi.org/10.1038/s41467-019-09020-4
Autor:
Kimberly Rizzolo, Sean Elliott
Publikováno v:
The FASEB Journal. 29
Recent bioinformatics analysis led to the discovery of unreported diheme enzymes found in all strains of Burkholderia, which share sequence similarity to known bacterial cytochrome c peroxidases (b...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::984655c8c9a2c0d646750f6190bab1bd
https://doi.org/10.1096/fasebj.29.1_supplement.573.24
https://doi.org/10.1096/fasebj.29.1_supplement.573.24