A single intersubunit salt bridge affects oligomerization and catalytic activity in a bacterial quinone reductase
dc.contributor.author | Binter, Alexandra | en_US |
dc.contributor.author | Staunig, Nicole | en_US |
dc.contributor.author | Jelesarov, Ilian | en_US |
dc.contributor.author | Lohner, Karl | en_US |
dc.contributor.author | Palfey, Bruce A. | en_US |
dc.contributor.author | Deller, Sigrid | en_US |
dc.contributor.author | Gruber, Karl F. | en_US |
dc.contributor.author | Macheroux, Peter | en_US |
dc.date.accessioned | 2010-06-01T21:27:16Z | |
dc.date.available | 2010-06-01T21:27:16Z | |
dc.date.issued | 2009-09 | en_US |
dc.identifier.citation | Binter, Alexandra; Staunig, Nicole; Jelesarov, Ilian; Lohner, Karl; Palfey, Bruce A.; Deller, Sigrid; Gruber, Karl; Macheroux, Peter (2009). "A single intersubunit salt bridge affects oligomerization and catalytic activity in a bacterial quinone reductase." FEBS Journal 276(18): 5263-5274. <http://hdl.handle.net/2027.42/74513> | en_US |
dc.identifier.issn | 1742-464X | en_US |
dc.identifier.issn | 1742-4658 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/74513 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=19682074&dopt=citation | en_US |
dc.format.extent | 831286 bytes | |
dc.format.extent | 3109 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.rights | Journal compilation © 2009 Federation of European Biochemical Societies | en_US |
dc.subject.other | NADPH:FMN Oxidoreductase | en_US |
dc.subject.other | Oligomerization | en_US |
dc.subject.other | Quinone Reductase | en_US |
dc.subject.other | Salt Bridge | en_US |
dc.subject.other | Thermostability | en_US |
dc.title | A single intersubunit salt bridge affects oligomerization and catalytic activity in a bacterial quinone reductase | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | 5 Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationother | 1 Institute of Biochemistry, Graz University of Technology, Austria | en_US |
dc.contributor.affiliationother | 2 Institute of Molecular Biosciences, University of Graz, Austria | en_US |
dc.contributor.affiliationother | 3 Institute of Biochemistry, University of ZÜrich, Switzerland | en_US |
dc.contributor.affiliationother | 4 Institute of Biophysics and Nanosystems Research, Austrian Academy of Sciences, Graz, Austria | en_US |
dc.identifier.pmid | 19682074 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/74513/1/j.1742-4658.2009.07222.x.pdf | |
dc.identifier.doi | 10.1111/j.1742-4658.2009.07222.x | en_US |
dc.identifier.source | FEBS Journal | en_US |
dc.identifier.citedreference | Bin Y, Jiti Z, Jing W, Cuihong D, Hongman H, Zhiyong S & Yongming B ( 2004 ) Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS1.1737. FEMS Microbiol Letters 236, 129 – 136. | en_US |
dc.identifier.citedreference | BlÜmel S, Knackmuss H-J & Stolz A ( 2002 ) Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F. Appl Environ Microbiol 68, 3948 – 3955. | en_US |
dc.identifier.citedreference | BlÜmel S & Stolz A ( 2003 ) Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24. Appl Microbiol Biotechnol 62, 186 – 190. | en_US |
dc.identifier.citedreference | Chen H, Hopper SL & Cerniglia CE ( 2005 ) Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein. Microbiology 151, 1433 – 1441. | en_US |
dc.identifier.citedreference | Chen H, Wang R-F & Cerniglia CE ( 2004 ) Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis. Protein Expr Purif 34, 302 – 310. | en_US |
dc.identifier.citedreference | Nakanishi M, Yatome C, Ishida N & Kitade Y ( 2001 ) Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase. J Biol Chem 276, 46394 – 46399. | en_US |
dc.identifier.citedreference | Suzuki Y, Yoda T, Ruhul A & Sugiura W ( 2001 ) Molecular cloning and characterisation of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil. J Biol Chem 276, 9059 – 9065. | en_US |
dc.identifier.citedreference | Deller S, Sollner S, Trenker-El-Toukhy R, Jelesarov I, Gubitz GM & Macheroux P ( 2006 ) Characterization of a thermostable NADPH:FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis. Biochemistry 45, 7083 – 7091. | en_US |
dc.identifier.citedreference | Deller S, Macheroux P & Sollner S ( 2008 ) Flavin-dependent quinone reductases. Cell Mol Life Sci 65, 141 – 160. | en_US |
dc.identifier.citedreference | Li R, Bianchet MA, Talalay P & Amzel LM ( 1995 ) The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc Natl Acad Sci USA 92, 8846 – 8850. | en_US |
dc.identifier.citedreference | Liger D, Graille M, Zhou C-Z, Leulliot N, Quevillon-Cheruel S, Blondeau K, Janin J & van Tilbeurgh H ( 2004 ) Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities. J Biol Chem 279, 34890 – 34897. | en_US |
dc.identifier.citedreference | Sollner S, Nebauer R, Ehammer H, Prem A, Deller S, Palfey BA, Daum G & Macheroux P ( 2007 ) Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification. FEBS J 274, 1328 – 1339. | en_US |
dc.identifier.citedreference | Dams T, Auerbach G, Bader G, Jacob U, Ploom T, Huber R & Jaenicke R ( 2000 ) The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability. J Mol Biol 297, 659 – 672. | en_US |
dc.identifier.citedreference | Murzin AG, Brenner SE, Hubbard T & Chothia C ( 1995 ) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247, 536 – 540. | en_US |
dc.identifier.citedreference | Krissinel E & Henrick K ( 2004 ) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr 60, 2256 – 2268. | en_US |
dc.identifier.citedreference | Agarwal R, Bonanno JB, Burley SK & Swaminathan S ( 2006 ) Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal. Acta Crystallogr 62, 383 – 391. | en_US |
dc.identifier.citedreference | Ye J, Yang HC, Rosen BP & Bhattacharjee H ( 2007 ) Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti. FEBS Lett 581, 3996 – 4000. | en_US |
dc.identifier.citedreference | Nissen MS, Youn B, Knowles BD, Ballinger JW, Jun SY, Belchik SM, Xun L & Kang C ( 2008 ) Crystal structures of NADH:FMN oxidoreductase (EmoB) at different stages of catalysis. J Biol Chem 283, 28710 – 28720. | en_US |
dc.identifier.citedreference | Vorontsov II, Minasov G, Brunzelle JS, Shuvalova L, Kiryukhina O, Collart FR & Anderson WF ( 2007 ) Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity. Protein Sci 16, 2483 – 2490. | en_US |
dc.identifier.citedreference | Krissinel E & Henrick K ( 2007 ) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372, 774 – 797. | en_US |
dc.identifier.citedreference | Thoma R, Hennig M, Sterner R & Kirschner K ( 2000 ) Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. Structure 8, 265 – 276. | en_US |
dc.identifier.citedreference | Walden H, Bell GS, Russell RJM, Siebers B, Hensel R & Taylor GL ( 2001 ) Tiny TIM: a small, tetrameric, hyperthermostable triosephosphate isomerase. J Mol Biol 306, 745 – 757. | en_US |
dc.identifier.citedreference | Ottolina G, Riva S, Carrea G, Danieli B & Buckmann AF ( 1989 ) Enzymatic synthesis of [4R-2H]NAD(P)H and [4S-2H]NAD(P)H and determination of the stereospecificity of 7 alpha- and 12 alpha hydroxysteroid dehydrogenase. Biochim Biophys Acta 998, 173 – 178. | en_US |
dc.identifier.citedreference | Otwinowski Z & Minor W ( 1997 ) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307 – 326. | en_US |
dc.identifier.citedreference | CCP4 ( 1994 ) The CCP4 suite – programs for protein crystallography. Acta Crystallogr 50, 760 – 763. | en_US |
dc.identifier.citedreference | McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC & Read RJ ( 2007 ) Phaser crystallographic software. J Appl Crystallogr 40, 658 – 674. | en_US |
dc.identifier.citedreference | Adams PD, Grosse-Kunstleve RW, Hung LW, Ioerger TR, McCoy AJ, Moriarty NW, Read RJ, Sacchettini JC, Sauter NK & Terwilliger TC ( 2002 ) PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr 58, 1948 – 1954. | en_US |
dc.identifier.citedreference | Emsley P & Cowtan K ( 2004 ) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60, 2126 – 2132. | en_US |
dc.identifier.citedreference | Read RJ ( 1986 ) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr 42, 140 – 149. | en_US |
dc.identifier.citedreference | Kleywegt GJ & Brunger AT ( 1996 ) Checking your imagination – applications of the free R-value. Structure 4, 897 – 904. | en_US |
dc.identifier.citedreference | Lovell SC, Davis IW, Arendall WB III, de Bakker PI, Word JM, Prisant MG, Richardson JS & Richardson DC ( 2003 ) Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins 50, 437 – 450. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.