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@article{903440, author = {Sedláček, Vojtěch and Kučera, Igor}, article_number = {11}, keywords = {metal bioreduction; flavoenzyme; flavin radical; oxidative stress}, language = {eng}, issn = {0302-8933}, journal = {Archives of microbiology}, title = {Chromate reductase activity of the Paracoccus denitrificans ferric reductase B (FerB) protein and its physiological relevance}, url = {http://www.springerlink.com/content/l424530251550087/fulltext.pdf}, volume = {192}, year = {2010} }
TY - JOUR ID - 903440 AU - Sedláček, Vojtěch - Kučera, Igor PY - 2010 TI - Chromate reductase activity of the Paracoccus denitrificans ferric reductase B (FerB) protein and its physiological relevance JF - Archives of microbiology VL - 192 IS - 11 SP - 919-926 EP - 919-926 PB - Springer SN - 03028933 KW - metal bioreduction KW - flavoenzyme KW - flavin radical KW - oxidative stress UR - http://www.springerlink.com/content/l424530251550087/fulltext.pdf N2 - The homodimeric flavoprotein FerB of Paracoccus denitrificans catalyzed the reduction of chromate with NADH as electron donor. When present, oxygen was reduced concomitantly with chromate. The recombinant enzyme had a maximum activity at pH 5.0. The stoichiometric ratio of NADH oxidized to chromate reduced was found to be 1.53 (O2 absent) or higher than 2 (O2 present), the apparent KM value for chromate amounted to 70 uM with the maximum rate of 2.9 umol NADH /s/(mg protein). Diode-array spectrophotometry and experiments with one-electron acceptors provided evidence for oxygen consumption being due to a flavin semiquinone, formed transiently during the interaction of FerB with chromate. At the whole-cell level, a ferB mutant strain displayed only slightly diminished rate of chromate reduction when compared to the wild-type parental strain. Anaerobically grown cells were more active than cells grown aerobically. The sensitivity to antimycin suggests an involvement of the respiratory chain. ER -
SEDLÁČEK, Vojtěch a Igor KUČERA. Chromate reductase activity of the Paracoccus denitrificans ferric reductase B (FerB) protein and its physiological relevance. \textit{Archives of microbiology}. Springer, 2010, roč.~192, č.~11, s.~919-926. ISSN~0302-8933.
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