%0 Journal Article %1 citeulike:519806 %A Hayashi, M. %A Nakayama, Y. %A Yasui, M. %A Maeda, M. %A Furuishi, K. %A Unemoto, T. %C Laboratory of Membrane Biochemistry, Faculty of Pharmaceutical Sciences, Chiba University, Chiba, Japan. makiha@p.chiba-u.ac.jp %D 2001 %J FEBS Lett %K flavin oxygenases maldi %N 1-2 %P 5--8 %T FMN is covalently attached to a threonine residue in the NqrB and NqrC subunits of Na(+)-translocating NADH-quinone reductase from Vibrio alginolyticus. %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11163785 %V 488 %X The Na(+)-translocating NADH-quinone reductase (NQR) from Vibrio alginolyticus is composed of six subunits (NqrA to NqrF). We previously demonstrated that both NqrB and NqrC subunits contain a flavin cofactor covalently attached to a threonine residue. Fluorescent peptide fragments derived from the NqrB and NqrC subunits were applied to a matrix-assisted laser desorption ionization time-of-flight mass spectrometer, and covalently attached flavin was identified as FMN in both subunits. From post-source decay fragmentation analysis, it was concluded that FMN is attached by a phosphate group to Thr-235 in the NqrB subunit and to Thr-223 in the NqrC subunit. The phosphoester binding of FMN to a threonine residue reported here is a new type of flavin attachment to a polypeptide.

@article{citeulike:519806, abstract = {The Na(+)-translocating NADH-quinone reductase (NQR) from Vibrio alginolyticus is composed of six subunits (NqrA to NqrF). We previously demonstrated that both NqrB and NqrC subunits contain a flavin cofactor covalently attached to a threonine residue. Fluorescent peptide fragments derived from the NqrB and NqrC subunits were applied to a matrix-assisted laser desorption ionization time-of-flight mass spectrometer, and covalently attached flavin was identified as FMN in both subunits. From post-source decay fragmentation analysis, it was concluded that FMN is attached by a phosphate group to Thr-235 in the NqrB subunit and to Thr-223 in the NqrC subunit. The phosphoester binding of FMN to a threonine residue reported here is a new type of flavin attachment to a polypeptide.}, added-at = {2007-02-02T11:54:15.000+0100}, address = {Laboratory of Membrane Biochemistry, Faculty of Pharmaceutical Sciences, Chiba University, Chiba, Japan. makiha@p.chiba-u.ac.jp}, author = {Hayashi, M. and Nakayama, Y. and Yasui, M. and Maeda, M. and Furuishi, K. and Unemoto, T.}, biburl = {https://www.bibsonomy.org/bibtex/2b18066a01dff9a5004d996376f3bb265/robert}, citeulike-article-id = {519806}, interhash = {5d88ba8f325e21e875591a5e890b46ff}, intrahash = {b18066a01dff9a5004d996376f3bb265}, issn = {0014-5793}, journal = {FEBS Lett}, keywords = {flavin oxygenases maldi}, month = {January}, number = {1-2}, pages = {5--8}, priority = {2}, timestamp = {2007-02-02T11:54:15.000+0100}, title = {FMN is covalently attached to a threonine residue in the NqrB and NqrC subunits of Na(+)-translocating NADH-quinone reductase from Vibrio alginolyticus.}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=11163785}, volume = 488, year = 2001 }