Další formáty:
BibTeX
LaTeX
RIS
@article{1545943, author = {Sedláček, Vojtěch and Kučera, Igor}, article_location = {Hoboken}, article_number = {7}, doi = {http://dx.doi.org/10.1002/1873-3468.13359}, keywords = {flavoprotein; antioxidant enzyme; chromate reductase; superoxide reductase}, language = {eng}, issn = {0014-5793}, journal = {FEBS Letters}, title = {Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans}, url = {https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13359}, volume = {593}, year = {2019} }
TY - JOUR ID - 1545943 AU - Sedláček, Vojtěch - Kučera, Igor PY - 2019 TI - Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans JF - FEBS Letters VL - 593 IS - 7 SP - 697-702 EP - 697-702 PB - Wiley SN - 00145793 KW - flavoprotein KW - antioxidant enzyme KW - chromate reductase KW - superoxide reductase UR - https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13359 L2 - https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13359 N2 - Ferric reductase B (FerB) is a flavin mononucleotide (FMN)containing NAD(P)H:acceptor oxidoreductase structurally close to the Gluconacetobacter hansenii chromate reductase (ChrR). The crystal structure of ChrR was previously determined with a chloride bound proximal to FMN in the vicinity of Arg101, and the authors suggested that the anionic electron acceptors, chromate and uranyl tricarbonate, bind similarly. Here, we identify the corresponding arginine residue in FerB (Arg95) as being important for the reaction of FerB with superoxide. Four mutants at position 95 were prepared and found kinetically to have impaired capacity for superoxide binding. Stopped flow data for the flavin cofactor showed that the oxidative step is rate limiting for catalytic turnover. The findings are consistent with a role for FerB as a superoxide scavenging contributor. ER -
SEDLÁČEK, Vojtěch a Igor KUČERA. Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans. \textit{FEBS Letters}. Hoboken: Wiley, 2019, roč.~593, č.~7, s.~697-702. ISSN~0014-5793. Dostupné z: https://dx.doi.org/10.1002/1873-3468.13359.
|