Holly R Ellis

Summary

Affiliation: College of Veterinary Medicine
Country: USA

Publications

  1. doi request reprint The FMN-dependent two-component monooxygenase systems
    Holly R Ellis
    The Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
    Arch Biochem Biophys 497:1-12. 2010
  2. pmc Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli
    Kholis Abdurachim
    Department of Chemistry and Biochemistry, Auburn University, 179 Chemistry Building, Auburn, AL 36849
    J Bacteriol 188:8153-9. 2006
  3. doi request reprint Mechanism for sulfur acquisition by the alkanesulfonate monooxygenase system
    Holly R Ellis
    The Department of Chemistry and Biochemistry, Auburn University, AL 36849, United States
    Bioorg Chem 39:178-84. 2011
  4. doi request reprint Deletional studies to investigate the functional role of a dynamic loop region of alkanesulfonate monooxygenase
    Jingyuan Xiong
    Department of Chemistry and Biochemistry, Auburn University, Auburn, AL, USA
    Biochim Biophys Acta 1824:898-906. 2012
  5. ncbi request reprint Mechanism of flavin reduction in the alkanesulfonate monooxygenase system
    Benlian Gao
    The Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
    Biochim Biophys Acta 1774:359-67. 2007
  6. doi request reprint Catalytic role of a conserved cysteine residue in the desulfonation reaction by the alkanesulfonate monooxygenase enzyme
    Russell A Carpenter
    The Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, USA
    Biochim Biophys Acta 1804:97-105. 2010
  7. ncbi request reprint Identification of critical steps governing the two-component alkanesulfonate monooxygenase catalytic mechanism
    John M Robbins
    Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
    Biochemistry 51:6378-87. 2012
  8. doi request reprint Catalytic importance of the substrate binding order for the FMNH2-dependent alkanesulfonate monooxygenase enzyme
    Xuanzhi Zhan
    Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, USA
    Biochemistry 47:2221-30. 2008
  9. doi request reprint Functional role of a conserved arginine residue located on a mobile loop of alkanesulfonate monooxygenase
    Russell A Carpenter
    Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, USA
    Biochemistry 50:6469-77. 2011
  10. doi request reprint Steady-state kinetic isotope effects support a complex role of Arg226 in the proposed desulfonation mechanism of alkanesulfonate monooxygenase
    John M Robbins
    Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, United States
    Biochemistry 53:161-8. 2014

Collaborators

  • P F Fitzpatrick
  • John M Robbins
  • Russell A Carpenter
  • Benlian Gao
  • Jingyuan Xiong
  • Xuanzhi Zhan
  • Erin M Imsand
  • Kholis Abdurachim
  • Catherine W Njeri
  • T Conn Mallett
  • William H Boles
  • Adam Bertrand

Detail Information

Publications14

  1. doi request reprint The FMN-dependent two-component monooxygenase systems
    Holly R Ellis
    The Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
    Arch Biochem Biophys 497:1-12. 2010
    ..This review covers the reported mechanistic and structural properties of these enzyme systems, and evaluates the mechanism of flavin transfer...
  2. pmc Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli
    Kholis Abdurachim
    Department of Chemistry and Biochemistry, Auburn University, 179 Chemistry Building, Auburn, AL 36849
    J Bacteriol 188:8153-9. 2006
    ..0022 +/- 0.0010 muM was obtained for the binding of SsuE to SsuD. Based on these studies, the stoichiometry for protein-protein interactions is proposed to involve a 1:1 monomeric association of SsuE with SsuD...
  3. doi request reprint Mechanism for sulfur acquisition by the alkanesulfonate monooxygenase system
    Holly R Ellis
    The Department of Chemistry and Biochemistry, Auburn University, AL 36849, United States
    Bioorg Chem 39:178-84. 2011
    ..This review discusses the physiological importance of this system, and the individual kinetic parameters and mechanistic properties of this enzyme system...
  4. doi request reprint Deletional studies to investigate the functional role of a dynamic loop region of alkanesulfonate monooxygenase
    Jingyuan Xiong
    Department of Chemistry and Biochemistry, Auburn University, Auburn, AL, USA
    Biochim Biophys Acta 1824:898-906. 2012
    ..These studies define the importance of dynamic loop region for protection and stabilization of reduced flavin and reaction intermediates...
  5. ncbi request reprint Mechanism of flavin reduction in the alkanesulfonate monooxygenase system
    Benlian Gao
    The Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
    Biochim Biophys Acta 1774:359-67. 2007
    ..While the utilization of flavin as a substrate by the alkanesulfonate monooxygenase system is novel, the mechanism for flavin reduction follows an analogous reaction path as standard flavoproteins...
  6. doi request reprint Catalytic role of a conserved cysteine residue in the desulfonation reaction by the alkanesulfonate monooxygenase enzyme
    Russell A Carpenter
    The Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, USA
    Biochim Biophys Acta 1804:97-105. 2010
    ..The data described suggest that Cys54 in SsuD may be either directly or indirectly involved in stabilizing the C4a-(hydro)peroxyflavin intermediate formed during catalysis through hydrogen bonding interactions...
  7. ncbi request reprint Identification of critical steps governing the two-component alkanesulfonate monooxygenase catalytic mechanism
    John M Robbins
    Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
    Biochemistry 51:6378-87. 2012
    ..5% of the wild-type SsuD k(cat) value. These results implicate Arg226 playing a critical role in catalysis and provide essential insights into the mechanistic steps that guide the SsuD desulfonation process...
  8. doi request reprint Catalytic importance of the substrate binding order for the FMNH2-dependent alkanesulfonate monooxygenase enzyme
    Xuanzhi Zhan
    Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, USA
    Biochemistry 47:2221-30. 2008
    ..These results suggest that an ordered substrate binding mechanism is important in the desulfonation reaction by SsuD with reduced flavin binding first followed by either O2 or octanesulfonate...
  9. doi request reprint Functional role of a conserved arginine residue located on a mobile loop of alkanesulfonate monooxygenase
    Russell A Carpenter
    Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, USA
    Biochemistry 50:6469-77. 2011
    ....
  10. doi request reprint Steady-state kinetic isotope effects support a complex role of Arg226 in the proposed desulfonation mechanism of alkanesulfonate monooxygenase
    John M Robbins
    Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, United States
    Biochemistry 53:161-8. 2014
    ....
  11. ncbi request reprint Altered mechanism of the alkanesulfonate FMN reductase with the monooxygenase enzyme
    Benlian Gao
    Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
    Biochem Biophys Res Commun 331:1137-45. 2005
    ..These results suggest that both the SsuD enzyme and alkanesulfonate substrate are required to ensure that the FMN reductase reaction proceeds to form the ternary complex with the subsequent generation of reduced flavin transfer...
  12. pmc Crystallization and preliminary X-ray crystallographic studies of the alkanesulfonate FMN reductase from Escherichia coli
    Benlian Gao
    Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
    Acta Crystallogr Sect F Struct Biol Cryst Commun 61:837-40. 2005
    ..It is anticipated that this new protein structure will provide detailed structural information on specific active-site regions of the protein and insight into the mechanism of flavin reduction and transfer of reduced flavin...
  13. doi request reprint Addition of an external electron donor to in vitro assays of cysteine dioxygenase precludes the need for exogenous iron
    Erin M Imsand
    Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849, USA
    Arch Biochem Biophys 521:10-7. 2012
    ..These studies shed light on the discrepancies among reported kinetic parameters for CDO and also juxtapose the stability of the 3-His and 2-His/1-carboxylate ferrous enzymes in the presence of dioxygen...
  14. ncbi request reprint Characterization of metal ligand mutants of tyrosine hydroxylase: insights into the plasticity of a 2-histidine-1-carboxylate triad
    Paul F Fitzpatrick
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, Texas 77843 2128, USA
    Biochemistry 42:2081-8. 2003
    ..In contrast, the H336E enzyme does not form a stable binary complex with dopamine, while the E376H and E376Q enzymes catalyze dopamine oxidation...