Cargando…
Inactivation of the Heme Degrading Enzyme IsdI by an Active Site Substitution That Diminishes Heme Ruffling
IsdG and IsdI are paralogous heme degrading enzymes from the bacterium Staphylococcus aureus. Heme bound by these enzymes is extensively ruffled such that the meso-carbons at the sites of oxidation are distorted toward bound oxygen. In contrast, the canonical heme oxygenase family degrades heme that...
Autores principales: | Ukpabi, Georgia, Takayama, Shin-ichi J., Mauk, A. Grant, Murphy, Michael E. P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3464526/ https://www.ncbi.nlm.nih.gov/pubmed/22891243 http://dx.doi.org/10.1074/jbc.M112.393249 |
Ejemplares similares
-
Heme ligation and redox chemistry in two bacterial thiosulfate dehydrogenase (TsdA) enzymes
por: Jenner, Leon P., et al.
Publicado: (2019) -
Secreted heme peroxidase from Dictyostelium discoideum: Insights into catalysis, structure, and biological role
por: Nicolussi, Andrea, et al.
Publicado: (2018) -
Regulatory mechanism of formaldehyde release in heme degradation catalyzed by Staphylococcus aureus IsdG
por: Matsui, Toshitaka
Publicado: (2023) -
Unique Heme-Iron Coordination by the Hemoglobin Receptor IsdB of Staphylococcus aureus
por: Gaudin, Catherine F. M., et al.
Publicado: (2011) -
Caspase-1 Promiscuity Is Counterbalanced by Rapid Inactivation of Processed Enzyme
por: Walsh, John G., et al.
Publicado: (2011)