F. Wayne Outten, PhD - Publications

Affiliations: 
2005- Chemistry and Biochemistry University of South Carolina, Columbia, SC 
Area:
Metal Ions in Biology
Website:
https://www.sc.edu/study/colleges_schools/artsandsciences/our-people/faculty-staff/outten_wayne.php

47 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 Blahut M, Sanchez E, Fisher CE, Outten FW. Fe-S Cluster Biogenesis by the Bacterial Suf Pathway. Biochimica Et Biophysica Acta. Molecular Cell Research. 118829. PMID 32822728 DOI: 10.1016/J.Bbamcr.2020.118829  1
2019 Blahut M, Wise CE, Bruno MR, Dong G, Makris TM, Frantom PA, Dunkle JA, Outten FW. Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues. The Journal of Biological Chemistry. PMID 31248989 DOI: 10.2210/Pdb6O11/Pdb  1
2018 Dunkle JA, Bruno M, Outten FW, Frantom PA. Structural evidence for dimer-interface driven regulation of the type II cysteine desulfurase, SufS. Biochemistry. PMID 30571100 DOI: 10.2210/Pdb6Mrh/Pdb  1
2018 Wofford JD, Bolaji N, Dziuba N, Outten FW, Lindahl PA. Evidence that a respiratory shield in protects a low-molecular-mass Fe pool from O-dependent oxidation. The Journal of Biological Chemistry. PMID 30337367 DOI: 10.1074/Jbc.Ra118.005233  0.08
2018 Washington-Hughes CL, Ford GT, Jones AD, McRae K, Outten FW. Nickel exposure reduces enterobactin production in Escherichia coli. Microbiologyopen. e00691. PMID 30062714 DOI: 10.1002/mbo3.691  0.01
2018 Blahut M, Dzul S, Wang S, Kandegedara A, Grossoehme NE, Stemmler T, Outten FW. Conserved cysteine residues are necessary for nickel-induced allosteric regulation of the metalloregulatory protein YqjI (NfeR) in E. coli. Journal of Inorganic Biochemistry. 184: 123-133. PMID 29723740 DOI: 10.1016/J.Jinorgbio.2018.04.016  1
2018 Kim D, Singh H, Dai Y, Dong G, Busenlehner LS, Outten FW, Frantom PA. Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems. Biochemistry. PMID 29589903 DOI: 10.1021/Acs.Biochem.7B01275  1
2016 Hanna DA, Harvey RM, Martinez-Guzman O, Yuan X, Chandrasekharan B, Raju G, Outten FW, Hamza I, Reddi AR. Heme dynamics and trafficking factors revealed by genetically encoded fluorescent heme sensors. Proceedings of the National Academy of Sciences of the United States of America. PMID 27247412 DOI: 10.1073/Pnas.1523802113  1
2015 Hirabayashi K, Yuda E, Tanaka N, Katayama S, Iwasaki K, Matsumoto T, Kurisu G, Outten FW, Fukuyama K, Takahashi Y, Wada K. Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis. The Journal of Biological Chemistry. PMID 26472926 DOI: 10.1074/Jbc.M115.680934  1
2015 Dai Y, Kim D, Dong G, Busenlehner LS, Frantom PA, Outten FW. SufE D74R Substitution Alters Active Site Loop Dynamics To Further Enhance SufE Interaction with the SufS Cysteine Desulfurase. Biochemistry. 54: 4824-33. PMID 26171726 DOI: 10.1021/Acs.Biochem.5B00663  1
2015 Wayne Outten F. Recent advances in the Suf Fe-S cluster biogenesis pathway: Beyond the Proteobacteria. Biochimica Et Biophysica Acta. 1853: 1464-9. PMID 25447545 DOI: 10.1016/J.Bbamcr.2014.11.001  0.24
2014 Boyd ES, Thomas KM, Dai Y, Boyd JM, Outten FW. Interplay between oxygen and Fe-S cluster biogenesis: insights from the Suf pathway. Biochemistry. 53: 5834-47. PMID 25153801 DOI: 10.1021/Bi500488R  1
2014 Wang S, Blahut M, Wu Y, Philipkosky KE, Outten FW. Communication between binding sites is required for yqjI regulation of target promoters within the yqjH-yqjI intergenic region Journal of Bacteriology. 196: 3199-3207. PMID 24982304 DOI: 10.1128/Jb.01835-14  1
2014 Outten FW. A stress-responsive Fe-S cluster biogenesis system in bacteria — the suf operon of gammaproteobacteria Iron-Sulfur Clusters in Chemistry and Biology. 297-324. DOI: 10.1515/9783110308426.297  1
2013 Singh H, Dai Y, Outten FW, Busenlehner LS. Escherichia coli sufe sulfur transfer protein modulates the sufs cysteine desulfurase through allosteric conformational dynamics Journal of Biological Chemistry. 288: 36189-36200. PMID 24196966 DOI: 10.1074/Jbc.M113.525709  1
2013 Wayne Outten F, Munson GP. Lability and liability of endogenous copper pools Journal of Bacteriology. 195: 4553-4555. PMID 23913325 DOI: 10.1128/Jb.00891-13  0.8
2012 Dai Y, Outten FW. The E. coli SufS-SufE sulfur transfer system is more resistant to oxidative stress than IscS-IscU Febs Letters. 586: 4016-4022. PMID 23068614 DOI: 10.1016/J.Febslet.2012.10.001  1
2012 Chahal HK, Outten FW. Separate FeS scaffold and carrier functions for SufB2C 2 and SufA during in vitro maturation of [2Fe2S] Fdx Journal of Inorganic Biochemistry. 116: 126-134. PMID 23018275 DOI: 10.1016/J.Jinorgbio.2012.06.008  1
2011 Wang S, Wu Y, Outten FW. Fur and the novel regulator yqji control transcription of the ferric reductase gene yqjh in escherichia coli Journal of Bacteriology. 193: 563-574. PMID 21097627 DOI: 10.1128/Jb.01062-10  1
2010 Saini A, Mapolelo DT, Chahal HK, Johnson MK, Outten FW. SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB. Biochemistry. 49: 9402-12. PMID 20857974 DOI: 10.1021/Bi1011546  1
2010 Saini A, Mapolelo DT, Chahal HK, Johnson MK, Outten FW. SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB. Biochemistry. 49: 9402-12. PMID 20857974 DOI: 10.1021/Bi1011546  1
2009 Chahal HK, Dai Y, Saini A, Ayala-Castro C, Outten FW. The SufBCD Fe-S scaffold complex interacts with sufa for Fe-s cluster transfer Biochemistry. 48: 10644-10653. PMID 19810706 DOI: 10.1021/Bi901518Y  1
2009 Gupta V, Sendra M, Naik SG, Chahal HK, Huynh BH, Outten FW, Fontecave M, De Choudens SO. Native escherichia coli SufA coexpressed with SufBCDSE purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes Journal of the American Chemical Society. 131: 6149-6153. PMID 19366265 DOI: 10.1021/Ja807551E  1
2009 Wada K, Sumi N, Nagai R, Iwasaki K, Sato T, Suzuki K, Hasegawa Y, Kitaoka S, Minami Y, Outten FW, Takahashi Y, Fukuyama K. Molecular Dynamism of Fe-S Cluster Biosynthesis Implicated by the Structure of the SufC2-SufD2 Complex Journal of Molecular Biology. 387: 245-258. PMID 19361433 DOI: 10.1016/J.Jmb.2009.01.054  1
2009 Wu Y, Outten FW. IscR controls iron-dependent biofilm formation in Escherichia coli by regulating type I fimbria expression Journal of Bacteriology. 191: 1248-1257. PMID 19074392 DOI: 10.1128/Jb.01086-08  1
2009 Outten FW, Theil EC. Iron-based redox switches in biology Antioxidants and Redox Signaling. 11: 1029-1046. PMID 19021503 DOI: 10.1089/Ars.2008.2296  1
2008 Mettert EL, Outten FW, Wanta B, Kiley PJ. The Impact of O2 on the Fe-S Cluster Biogenesis Requirements of Escherichia coli FNR Journal of Molecular Biology. 384: 798-811. PMID 18938178 DOI: 10.1016/J.Jmb.2008.09.080  1
2008 Ayala-Castro C, Saini A, Outten FW. Fe-S cluster assembly pathways in bacteria Microbiology and Molecular Biology Reviews. 72: 110-125. PMID 18322036 DOI: 10.1128/Mmbr.00034-07  1
2007 Outten FW. Iron-sulfur clusters as oxygen-responsive molecular switches Nature Chemical Biology. 3: 206-207. PMID 17372605 DOI: 10.1038/Nchembio0407-206  1
2007 Layer G, Aparna Gaddam S, Ayala-Castro CN, Choudens SOD, Lascoux D, Fontecave M, Outten FW. SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly Journal of Biological Chemistry. 282: 13342-13350. PMID 17350958 DOI: 10.1074/Jbc.M608555200  1
2006 Wang X, Mukhopadhyay P, Wood MJ, Outten FW, Opdyke JA, Storz G. Mutational analysis to define an activating region on the redox-sensitive transcriptional regulator OxyR. Journal of Bacteriology. 188: 8335-42. PMID 17012382 DOI: 10.1128/Jb.01318-06  1
2006 Wang X, Mukhopadhyay P, Wood MJ, Outten FW, Opdyke JA, Storz G. Mutational analysis to define an activating region on the redox-sensitive transcriptional regulator OxyR. Journal of Bacteriology. 188: 8335-42. PMID 17012382 DOI: 10.1128/Jb.01318-06  1
2004 Djaman O, Outten FW, Imlay JA. Repair of oxidized iron-sulfur clusters in Escherichia coli Journal of Biological Chemistry. 279: 44590-44599. PMID 15308657 DOI: 10.1074/Jbc.M406487200  1
2004 Outten FW, Djaman O, Storz G. A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli Molecular Microbiology. 52: 861-872. PMID 15101990 DOI: 10.1111/J.1365-2958.2004.04025.X  1
2003 Outten FW, Wood MJ, Munoz FM, Storz G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. The Journal of Biological Chemistry. 278: 45713-9. PMID 12941942 DOI: 10.1074/Jbc.M308004200  1
2003 Outten FW, Wood MJ, Munoz FM, Storz G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. The Journal of Biological Chemistry. 278: 45713-9. PMID 12941942 DOI: 10.1074/Jbc.M308004200  1
2002 Huffman DL, Huyett J, Outten FW, Doan PE, Finney LA, Hoffman BM, O'Halloran TV. Spectroscopy of Cu(II)-PcoC and the multicopper oxidase function of PcoA, two essential components of Escherichia coli pco copper resistance operon. Biochemistry. 41: 10046-55. PMID 12146969 DOI: 10.1021/Bi0259960  1
2002 Huffman DL, Huyett J, Outten FW, Doan PE, Finney LA, Hoffman BM, O'Halloran TV. Spectroscopy of Cu(II)-PcoC and the multicopper oxidase function of PcoA, two essential components of Escherichia coli pco copper resistance operon. Biochemistry. 41: 10046-55. PMID 12146969 DOI: 10.1021/Bi0259960  1
2001 Outten FW, Huffman DL, Hale JA, O'Halloran TV. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. The Journal of Biological Chemistry. 276: 30670-7. PMID 11399769 DOI: 10.1074/Jbc.M104122200  1
2001 Outten FW, Huffman DL, Hale JA, O'Halloran TV. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. The Journal of Biological Chemistry. 276: 30670-7. PMID 11399769 DOI: 10.1074/Jbc.M104122200  1
2000 Munson GP, Lam DL, Outten FW, O'Halloran TV. Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12. Journal of Bacteriology. 182: 5864-71. PMID 11004187 DOI: 10.1128/Jb.182.20.5864-5871.2000  1
2000 Munson GP, Lam DL, Outten FW, O'Halloran TV. Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12. Journal of Bacteriology. 182: 5864-71. PMID 11004187 DOI: 10.1128/Jb.182.20.5864-5871.2000  1
2000 Outten FW, Outten CE, Hale J, O'Halloran TV. Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, cueR. The Journal of Biological Chemistry. 275: 31024-9. PMID 10915804 DOI: 10.1074/Jbc.M006508200  1
2000 Outten FW, Outten CE, Hale J, O'Halloran TV. Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, cueR. The Journal of Biological Chemistry. 275: 31024-9. PMID 10915804 DOI: 10.1074/Jbc.M006508200  1
1999 Outten CE, Outten FW, O'Halloran TV. DNA distortion mechanism for transcriptional activation by ZntR, a Zn(II)-responsive MerR homologue in Escherichia coli. The Journal of Biological Chemistry. 274: 37517-24. PMID 10608803 DOI: 10.1074/Jbc.274.53.37517  1
1999 Outten CE, Outten FW, O'Halloran TV. DNA distortion mechanism for transcriptional activation by ZntR, a Zn(II)-responsive MerR homologue in Escherichia coli. The Journal of Biological Chemistry. 274: 37517-24. PMID 10608803 DOI: 10.1074/Jbc.274.53.37517  1
1997 Scholnick J, Sinor C, Oakes J, Outten W, Saha M. Differential expression of Xenopus ribosomal protein gene XlrpS1c Biochimica Et Biophysica Acta - Gene Structure and Expression. 1354: 72-82. PMID 9375795 DOI: 10.1016/S0167-4781(97)00101-2  0.36
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