Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center

York, Nicholas J.; Lockart, Molly M.; Sardar, Sinjinee; Khadka, Nimesh; Shi, Wuxian; Stenkamp, Ronald E.; Zhang, Jianye; Kiser, Philip D.; Pierce, Brad S.

doi:10.1016/j.jbc.2021.100492

Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center

Journal Article · Fri Jan 01 00:00:00 EST 2021 · Journal of Biological Chemistry

DOI:https://doi.org/10.1016/j.jbc.2021.100492· OSTI ID:1778798

^[1]; Lockart, Molly M. ^[1]; Sardar, Sinjinee ^[2]; Khadka, Nimesh ^[3]; Shi, Wuxian ^[4]; ^[5]; Zhang, Jianye ^[6]; ^[7]; ^[1]

Univ. of Alabama, Birmingham, AL (United States). Dept. of Chemistry and Biochemistry
Univ. of Texas, Arlington, TX (United States). Dept. of Chemistry and Biochemistry
Case Western Reserve Univ., Cleveland, OH (United States). Dept. of Pharmacology
Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source II (NSLS-II)
Univ. of Washington, Seattle, WA (United States). Depts. of Biological Structure and Biochemistry
Univ. of California, Irvine, CA (United States). School of Medicine, Dept. of Ophthalmology
Univ. of California, Irvine, CA (United States). School of Medicine, Dept. of Ophthalmology; Univ. of California, Irvine, CA (United States). School of Medicine, Dept. of Physiology and Biophysics; VA Long Beach Healthcare System, CA (United States). Research Service

Thiol dioxygenases are a subset of nonheme iron oxygenases that catalyze the formation of sulfinic acids from sulfhydryl-containing substrates and dioxygen. Among this class, cysteine dioxygenases (CDOs) and 3-mercaptopropionic acid dioxygenases (3MDOs) are the best characterized, and the mode of substrate binding for CDOs is well understood. However, the manner in which 3-mercaptopropionic acid (3MPA) coordinates to the nonheme iron site in 3MDO remains a matter of debate. A model for bidentate 3MPA coordination at the 3MDO Fe-site has been proposed on the basis of computational docking, whereas steady-state kinetics and EPR spectroscopic measurements suggest a thiolate-only coordination of the substrate. To address this gap in knowledge, we determined the structure of Azobacter vinelandii 3MDO (Av3MDO) in complex with the substrate analog and competitive inhibitor, 3-hydroxypropionic acid (3HPA). The structure together with DFT computational modeling demonstrates that 3HPA and 3MPA associate with iron as chelate complexes with the substrate-carboxylate group forming an additional interaction with Arg168 and the thiol bound at the same position as in CDO. A chloride ligand was bound to iron in the coordination site assigned as the O₂-binding site. Supporting HYSCORE spectroscopic experiments were performed on the (3MPA/NO)-bound Av3MDO iron nitrosyl (S = 3/2) site. In combination with spectroscopic simulations and optimized DFT models, this work provides an experimentally verified model of the Av3MDO enzyme–substrate complex, effectively resolving a debate in the literature regarding the preferred substrate-binding denticity. These results elegantly explain the observed 3MDO substrate specificity, but leave unanswered questions regarding the mechanism of substrate-gated reactivity with dioxygen.

View Accepted Manuscript (DOE)

Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)

Grant/Contract Number:: SC0012704

OSTI ID:: 1778798

Alternate ID(s):: OSTI ID: 1777300

Report Number(s):: BNL--221309-2021-JAAM

Journal Information:: Journal of Biological Chemistry, Journal Name: Journal of Biological Chemistry Vol. 296; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: English

References (88)

UCSF Chimera?A visualization system for exploratory research and analysis Pettersen, Eric F.; Goddard, Thomas D.; Huang, Conrad C. Journal of Computational Chemistry, Vol. 25, Issue 13 https://doi.org/10.1002/jcc.20084	journal	January 2004
Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs: Arg- and Gln-type Bacterial CDO Homologs Driggers, Camden M.; Hartman, Steven J.; Karplus, P. Andrew Protein Science, Vol. 24, Issue 1 https://doi.org/10.1002/pro.2587	journal	November 2014
MolProbity: More and better reference data for improved all-atom structure validation: PROTEIN SCIENCE.ORG Williams, Christopher J.; Headd, Jeffrey J.; Moriarty, Nigel W. Protein Science, Vol. 27, Issue 1 https://doi.org/10.1002/pro.3330	journal	November 2017
The impact of the resolution of the identity approximate integral method on modern ab initio algorithm development Kendall, Rick A.; Früchtl, Herbert A. Theoretical Chemistry Accounts: Theory, Computation, and Modeling (Theoretica Chimica Acta), Vol. 97, Issue 1-4 https://doi.org/10.1007/s002140050249	journal	October 1997
1H-HYSCORE Reveals Structural Details at the Fe(II) Active Site of Taurine:2-Oxoglutarate Dioxygenase McCracken, John; Casey, Thomas M.; Hausinger, Robert P. Applied Magnetic Resonance https://doi.org/10.1007/s00723-020-01288-w	journal	October 2020
Computational study of the electronic structure and magnetic properties of the Ni–C state in [NiFe] hydrogenases including the second coordination sphere Kampa, Mario; Lubitz, Wolfgang; van Gastel, Maurice JBIC Journal of Biological Inorganic Chemistry, Vol. 17, Issue 8 https://doi.org/10.1007/s00775-012-0941-9	journal	October 2012
Heme-bound nitroxyl, hydroxylamine, and ammonia ligands as intermediates in the reaction cycle of cytochrome c nitrite reductase: a theoretical study Bykov, Dmytro; Plog, Matthias; Neese, Frank JBIC Journal of Biological Inorganic Chemistry, Vol. 19, Issue 1 https://doi.org/10.1007/s00775-013-1065-6	journal	November 2013
Influence of cysteine 164 on active site structure in rat cysteine dioxygenase Fellner, Matthias; Siakkou, Eleni; Faponle, Abayomi S. JBIC Journal of Biological Inorganic Chemistry, Vol. 21, Issue 4 https://doi.org/10.1007/s00775-016-1360-0	journal	May 2016
Determination of the pKa value of the hydroxyl group in the α-hydroxycarboxylates citrate, malate and lactate by 13C NMR: implications for metal coordination in biological systems Silva, Andre M. N.; Kong, Xiaole; Hider, Robert C. BioMetals, Vol. 22, Issue 5 https://doi.org/10.1007/s10534-009-9224-5	journal	March 2009
The enzymatic oxidation of cysteine to cysteinesulfinate in rat liver Sörbo, Bo; Ewetz, Lena Biochemical and Biophysical Research Communications, Vol. 18, Issue 3 https://doi.org/10.1016/0006-291X(65)90714-X	journal	February 1965
Integral approximations for LCAO-SCF calculations Vahtras, O.; Almlöf, J.; Feyereisen, M. W. Chemical Physics Letters, Vol. 213, Issue 5-6 https://doi.org/10.1016/0009-2614(93)89151-7	journal	October 1993
Abnormal sulphur oxidation in systemic lupus erythematosus Gordon, C.; Emery, P.; Bradley, H. The Lancet, Vol. 339, Issue 8784 https://doi.org/10.1016/0140-6736(92)90144-R	journal	January 1992
Plasma cysteine and sulphate levels in patients with motor neurone, Parkinson's and Alzheimer's disease Heafield, M. Thomas; Fearn, Simon; Steventon, Glyn B. Neuroscience Letters, Vol. 110, Issue 1-2 https://doi.org/10.1016/0304-3940(90)90814-P	journal	March 1990
Characteristics of the cysteinesulfinate-forming enzyme system in rat liver Ewetz, Lena; Sörbo, Bo Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, Vol. 128, Issue 2 https://doi.org/10.1016/0926-6593(66)90176-7	journal	November 1966
Principles of structure, bonding, and reactivity for metal nitrosyl complexes Enemark, J. H.; Feltham, R. D. Coordination Chemistry Reviews, Vol. 13, Issue 4 https://doi.org/10.1016/S0010-8545(00)80259-3	journal	September 1974
EPR and Mössbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environment. Arciero, D. M.; Lipscomb, J. D.; Huynh, B. H. Journal of Biological Chemistry, Vol. 258, Issue 24 https://doi.org/10.1016/S0021-9258(17)43760-4	journal	December 1983
Ligation of the diiron site of the hydroxylase component of methane monooxygenase. An electron nuclear double resonance study. Hendrich, M. P.; Fox, B. G.; Andersson, K. K. Journal of Biological Chemistry, Vol. 267, Issue 1 https://doi.org/10.1016/S0021-9258(18)48488-8	journal	January 1992
Cysteine Oxygenase Lombardini, J. B.; Singer, T. P.; Boyer, P. D. Journal of Biological Chemistry, Vol. 244, Issue 5 https://doi.org/10.1016/S0021-9258(18)91825-9	journal	March 1969
Plasticity of enzyme active sites Todd, Annabel E.; Orengo, Christine A.; Thornton, Janet M. Trends in Biochemical Sciences, Vol. 27, Issue 8 https://doi.org/10.1016/S0968-0004(02)02158-8	journal	August 2002
Shifting redox states of the iron center partitions CDO between crosslink formation or cysteine oxidation Njeri, Catherine W.; Ellis, Holly R. Archives of Biochemistry and Biophysics, Vol. 558 https://doi.org/10.1016/j.abb.2014.06.001	journal	September 2014
Steady-state substrate specificity and O2-coupling efficiency of mouse cysteine dioxygenase Li, Wei; Pierce, Brad S. Archives of Biochemistry and Biophysics, Vol. 565 https://doi.org/10.1016/j.abb.2014.11.004	journal	January 2015
Non-chemical proton-dependent steps prior to O2-activation limit Azotobacter vinelandii 3-mercaptopropionic acid dioxygenase (MDO) catalysis Crowell, Joshua K.; Sardar, Sinjinee; Hossain, Mohammad S. Archives of Biochemistry and Biophysics, Vol. 604 https://doi.org/10.1016/j.abb.2016.06.009	journal	August 2016
Thiol dioxygenase turnover yields benzothiazole products from 2-mercaptoaniline and O2-dependent oxidation of primary alcohols Morrow, William P.; Sardar, Sinjinee; Thapa, Pawan Archives of Biochemistry and Biophysics, Vol. 631 https://doi.org/10.1016/j.abb.2017.08.013	journal	October 2017
Recent advances in biological production of 3-hydroxypropionic acid Kumar, Vinod; Ashok, Somasundar; Park, Sunghoon Biotechnology Advances, Vol. 31, Issue 6 https://doi.org/10.1016/j.biotechadv.2013.02.008	journal	November 2013
Expanding the functional diversity of proteins through cysteine oxidation Reddie, Khalilah G.; Carroll, Kate S. Current Opinion in Chemical Biology, Vol. 12, Issue 6 https://doi.org/10.1016/j.cbpa.2008.07.028	journal	December 2008
Efficient, approximate and parallel Hartree–Fock and hybrid DFT calculations. A ‘chain-of-spheres’ algorithm for the Hartree–Fock exchange Neese, Frank; Wennmohs, Frank; Hansen, Andreas Chemical Physics, Vol. 356, Issue 1-3 https://doi.org/10.1016/j.chemphys.2008.10.036	journal	February 2009
Inference of Macromolecular Assemblies from Crystalline State Krissinel, Evgeny; Henrick, Kim Journal of Molecular Biology, Vol. 372, Issue 3 https://doi.org/10.1016/j.jmb.2007.05.022	journal	September 2007
Cysteine Dioxygenase Structures from pH4 to 9: Consistent Cys-Persulfenate Formation at Intermediate pH and a Cys-Bound Enzyme at Higher pH Driggers, Camden M.; Cooley, Richard B.; Sankaran, Banumathi Journal of Molecular Biology, Vol. 425, Issue 17 https://doi.org/10.1016/j.jmb.2013.05.028	journal	September 2013
Structure-Based Insights into the Role of the Cys–Tyr Crosslink and Inhibitor Recognition by Mammalian Cysteine Dioxygenase Driggers, Camden M.; Kean, Kelsey M.; Hirschberger, Lawrence L. Journal of Molecular Biology, Vol. 428, Issue 20 https://doi.org/10.1016/j.jmb.2016.07.012	journal	October 2016
EasySpin, a comprehensive software package for spectral simulation and analysis in EPR Stoll, Stefan; Schweiger, Arthur Journal of Magnetic Resonance, Vol. 178, Issue 1, p. 42-55 https://doi.org/10.1016/j.jmr.2005.08.013	journal	January 2006
How environmental and genetic factors combine to cause autism: A redox/methylation hypothesis Deth, Richard; Muratore, Christina; Benzecry, Jorge NeuroToxicology, Vol. 29, Issue 1 https://doi.org/10.1016/j.neuro.2007.09.010	journal	January 2008
Mononuclear and dinuclear iron thiocyanate and selenocyanate complexes of tris-pyrazolylmethane ligands Abibat Salaudeen, A.; Kilner, Colin A.; Halcrow, Malcolm A. Polyhedron, Vol. 27, Issue 12 https://doi.org/10.1016/j.poly.2008.05.013	journal	August 2008
A New Generation of Crystallographic Validation Tools for the Protein Data Bank Read, Randy J.; Adams, Paul D.; Arendall, W. Bryan Structure, Vol. 19, Issue 10 https://doi.org/10.1016/j.str.2011.08.006	journal	October 2011
Oxidative activation of antioxidant defence Winyard, Paul G.; Moody, Christopher J.; Jacob, Claus Trends in Biochemical Sciences, Vol. 30, Issue 8 https://doi.org/10.1016/j.tibs.2005.06.001	journal	August 2005
Spectroscopic Investigation of Cysteamine Dioxygenase Fernandez, Rebeca L.; Dillon, Stephanie L.; Stipanuk, Martha H. Biochemistry, Vol. 59, Issue 26 https://doi.org/10.1021/acs.biochem.0c00267	journal	June 2020
Spectroscopic and Computational Investigation of the H155A Variant of Cysteine Dioxygenase: Geometric and Electronic Consequences of a Third-Sphere Amino Acid Substitution Blaesi, Elizabeth J.; Fox, Brian G.; Brunold, Thomas C. Biochemistry, Vol. 54, Issue 18 https://doi.org/10.1021/acs.biochem.5b00171	journal	April 2015
HYSCORE Analysis of the Effects of Substrates on Coordination of Water to the Active Site Iron in Tyrosine Hydroxylase McCracken, John; Eser, Bekir E.; Mannikko, Donald Biochemistry, Vol. 54, Issue 24 https://doi.org/10.1021/acs.biochem.5b00363	journal	June 2015
The “Gln-Type” Thiol Dioxygenase from Azotobacter vinelandii Is a 3-Mercaptopropionic Acid Dioxygenase Pierce, Brad S.; Subedi, Bishnu P.; Sardar, Sinjinee Biochemistry, Vol. 54, Issue 51 https://doi.org/10.1021/acs.biochem.5b00636	journal	December 2015
Substrate and pH-Dependent Kinetic Profile of 3-Mercaptopropionate Dioxygenase from Pseudomonas aeruginosa Fellner, Matthias; Aloi, Sekotilani; Tchesnokov, Egor P. Biochemistry, Vol. 55, Issue 9 https://doi.org/10.1021/acs.biochem.5b01203	journal	February 2016
Substrate Specificity in Thiol Dioxygenases Aloi, Sekotilani; Davies, Casey G.; Karplus, P. Andrew Biochemistry, Vol. 58, Issue 19 https://doi.org/10.1021/acs.biochem.9b00079	journal	April 2019
Outer-Sphere Tyrosine 159 within the 3-Mercaptopropionic Acid Dioxygenase S-H-Y Motif Gates Substrate-Coordination Denticity at the Non-Heme Iron Active Site Sardar, Sinjinee; Weitz, Andrew; Hendrich, Michael P. Biochemistry, Vol. 58, Issue 51 https://doi.org/10.1021/acs.biochem.9b00674	journal	November 2019
Synthesis, X-ray Structures, Electronic Properties, and O ₂ /NO Reactivities of Thiol Dioxygenase Active-Site Models Fischer, Anne A.; Stracey, Nuru; Lindeman, Sergey V. Inorganic Chemistry, Vol. 55, Issue 22 https://doi.org/10.1021/acs.inorgchem.6b01931	journal	November 2016
Spectroscopic and Computational Comparisons of Thiolate-Ligated Ferric Nonheme Complexes to Cysteine Dioxygenase: Second-Sphere Effects on Substrate (Analogue) Positioning Fischer, Anne A.; Miller, Joshua R.; Jodts, Richard J. Inorganic Chemistry, Vol. 58, Issue 24 https://doi.org/10.1021/acs.inorgchem.9b02432	journal	November 2019
Second-Sphere Interactions between the C93–Y157 Cross-Link and the Substrate-Bound Fe Site Influence the O ₂ Coupling Efficiency in Mouse Cysteine Dioxygenase Li, Wei; Blaesi, Elizabeth J.; Pecore, Michael D. Biochemistry, Vol. 52, Issue 51 https://doi.org/10.1021/bi4010232	journal	November 2013
Oxidative Uncoupling in Cysteine Dioxygenase Is Gated by a Proton-Sensitive Intermediate Crowell, Joshua K.; Li, Wei; Pierce, Brad S. Biochemistry, Vol. 53, Issue 48 https://doi.org/10.1021/bi501241d	journal	November 2014
The Cys-Tyr Cross-Link of Cysteine Dioxygenase Changes the Optimal pH of the Reaction without a Structural Change Davies, Casey G.; Fellner, Matthias; Tchesnokov, Egor P. Biochemistry, Vol. 53, Issue 50 https://doi.org/10.1021/bi501277a	journal	December 2014
Characterization of the Nitrosyl Adduct of Substrate-Bound Mouse Cysteine Dioxygenase by Electron Paramagnetic Resonance: Electronic Structure of the Active Site and Mechanistic Implications ^† Pierce, Brad S.; Gardner, Jessica D.; Bailey, Lucas J. Biochemistry, Vol. 46, Issue 29 https://doi.org/10.1021/bi700662d	journal	July 2007
Geometries of Transition-Metal Complexes from Density-Functional Theory Bühl, Michael; Kabrede, Hendrik Journal of Chemical Theory and Computation, Vol. 2, Issue 5 https://doi.org/10.1021/ct6001187	journal	June 2006
Modulation of the p K _a of Metal-Bound Water via Oxidation of Thiolato Sulfur in Model Complexes of Co(III) Containing Nitrile Hydratase: Insight into Possible Effect of Cysteine Oxidation in Co−Nitrile Hydratase Tyler, Laurie A.; Noveron, Juan C.; Olmstead, Marilyn M. Inorganic Chemistry, Vol. 42, Issue 18 https://doi.org/10.1021/ic030088s	journal	September 2003
Calibration of Modern Density Functional Theory Methods for the Prediction of ⁵⁷ Fe Mössbauer Isomer Shifts: Meta-GGA and Double-Hybrid Functionals Römelt, Michael; Ye, Shengfa; Neese, Frank Inorganic Chemistry, Vol. 48, Issue 3 https://doi.org/10.1021/ic801535v	journal	February 2009
VTVH-MCD and DFT Studies of Thiolate Bonding to {FeNO} ⁷ /{FeO ₂ } ⁸ Complexes of Isopenicillin N Synthase: Substrate Determination of Oxidase versus Oxygenase Activity in Nonheme Fe Enzymes Brown, Christina D.; Neidig, Michael L.; Neibergall, Matthew B. Journal of the American Chemical Society, Vol. 129, Issue 23 https://doi.org/10.1021/ja071364v	journal	June 2007
Water-Soluble Fe(II)–H ₂ O Complex with a Weak O–H Bond Transfers a Hydrogen Atom via an Observable Monomeric Fe(III)–OH Brines, Lisa M.; Coggins, Michael K.; Poon, Penny Chaau Yan Journal of the American Chemical Society, Vol. 137, Issue 6 https://doi.org/10.1021/ja5068405	journal	February 2015
Cryoreduction of the NO-Adduct of Taurine:α-Ketoglutarate Dioxygenase (TauD) Yields an Elusive {FeNO} ⁸ Species Ye, Shengfa; Price, John C.; Barr, Eric W. Journal of the American Chemical Society, Vol. 132, Issue 13 https://doi.org/10.1021/ja909715g	journal	March 2010
Two-Dimensional ESEEM Spectroscopy of Nitrogen Hyperfine Couplings in Methemerythrin and Azidomethemerythrin Dikanov, Sergei A.; Davydov, Roman M.; Gräslund, Astrid Journal of the American Chemical Society, Vol. 120, Issue 27 https://doi.org/10.1021/ja9742343	journal	July 1998
Experimental Correlation of Substrate Position with Reaction Outcome in the Aliphatic Halogenase, SyrB2 Martinie, Ryan J.; Livada, Jovan; Chang, Wei-chen Journal of the American Chemical Society, Vol. 137, Issue 21 https://doi.org/10.1021/jacs.5b03370	journal	May 2015
Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase Mitchell, Andrew J.; Dunham, Noah P.; Martinie, Ryan J. Journal of the American Chemical Society, Vol. 139, Issue 39 https://doi.org/10.1021/jacs.7b07374	journal	September 2017
Structures, Spectroscopic Properties, and Dioxygen Reactivity of 5- and 6-Coordinate Nonheme Iron(II) Complexes: A Combined Enzyme/Model Study of Thiol Dioxygenases Gordon, Jesse B.; McGale, Jeremy P.; Prendergast, Joshua R. Journal of the American Chemical Society, Vol. 140, Issue 44 https://doi.org/10.1021/jacs.8b08349	journal	October 2018
Elucidating the Reaction Pathway of Decarboxylation-Assisted Olefination Catalyzed by a Mononuclear Non-Heme Iron Enzyme Yu, Cheng-Ping; Tang, Yijie; Cha, Lide Journal of the American Chemical Society, Vol. 140, Issue 45 https://doi.org/10.1021/jacs.8b10077	journal	October 2018
Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets White, Mark D.; Klecker, Maria; Hopkinson, Richard J. Nature Communications, Vol. 8, Issue 1 https://doi.org/10.1038/ncomms14690	journal	March 2017
Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway Weits, Daan A.; Giuntoli, Beatrice; Kosmacz, Monika Nature Communications, Vol. 5, Issue 1 https://doi.org/10.1038/ncomms4425	journal	March 2014
Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach? Trachootham, Dunyaporn; Alexandre, Jerome; Huang, Peng Nature Reviews Drug Discovery, Vol. 8, Issue 7 https://doi.org/10.1038/nrd2803	journal	May 2009
Balanced basis sets of split valence, triple zeta valence and quadruple zeta valence quality for H to Rn: Design and assessment of accuracy Weigend, Florian; Ahlrichs, Reinhart Physical Chemistry Chemical Physics, Vol. 7, Issue 18, p. 3297-3305 https://doi.org/10.1039/b508541a	journal	January 2005
Studies on the relationship between chemical constitution and physiological action Easson, Leslie Hilton; Stedman, Edgar Biochemical Journal, Vol. 27, Issue 4 https://doi.org/10.1042/bj0271257	journal	January 1933
A consistent and accurate ab initio parametrization of density functional dispersion correction (DFT-D) for the 94 elements H-Pu Grimme, Stefan; Antony, Jens; Ehrlich, Stephan The Journal of Chemical Physics, Vol. 132, Issue 15 https://doi.org/10.1063/1.3382344	journal	April 2010
Density functional calculations of molecular bond energies Becke, A. D. The Journal of Chemical Physics, Vol. 84, Issue 8 https://doi.org/10.1063/1.450025	journal	April 1986
Structure and mechanism of mouse cysteine dioxygenase McCoy, J. G.; Bailey, L. J.; Bitto, E. Proceedings of the National Academy of Sciences, Vol. 103, Issue 9 https://doi.org/10.1073/pnas.0509262103	journal	February 2006
Mercaptosuccinate Dioxygenase, a Cysteine Dioxygenase Homologue, from Variovorax paradoxus Strain B4 Is the Key Enzyme of Mercaptosuccinate Degradation Brandt, Ulrike; Schürmann, Marc; Steinbüchel, Alexander Journal of Biological Chemistry, Vol. 289, Issue 44 https://doi.org/10.1074/jbc.M114.579730	journal	October 2014
The Cysteine Dioxygenase Homologue from Pseudomonas aeruginosa Is a 3-Mercaptopropionate Dioxygenase Tchesnokov, Egor P.; Fellner, Matthias; Siakkou, Eleni Journal of Biological Chemistry, Vol. 290, Issue 40 https://doi.org/10.1074/jbc.M114.635672	journal	October 2015
Direct evidence that an extended hydrogen-bonding network influences activation of pyridoxal 5′-phosphate in aspartate aminotransferase Dajnowicz, Steven; Parks, Jerry M.; Hu, Xiche Journal of Biological Chemistry, Vol. 292, Issue 14 https://doi.org/10.1074/jbc.M116.774588	journal	February 2017
Crystal Structure of Mammalian Cysteine Dioxygenase: A NOVEL MONONUCLEAR IRON CENTER FOR CYSTEINE THIOL OXIDATION Simmons, Chad R.; Liu, Qun; Huang, Qingqiu Journal of Biological Chemistry, Vol. 281, Issue 27 https://doi.org/10.1074/jbc.M601555200	journal	April 2006
An Insight into the Mechanism of Human Cysteine Dioxygenase: KEY ROLES OF THE THIOETHER-BONDED TYROSINE-CYSTEINE COFACTOR Ye, Sheng; Wu, Xiao'ai; Wei, Lei Journal of Biological Chemistry, Vol. 282, Issue 5 https://doi.org/10.1074/jbc.M609337200	journal	November 2006
Discovery and Characterization of a Second Mammalian Thiol Dioxygenase, Cysteamine Dioxygenase Dominy, John E.; Simmons, Chad R.; Hirschberger, Lawrence L. Journal of Biological Chemistry, Vol. 282, Issue 35 https://doi.org/10.1074/jbc.M703089200	journal	August 2007
Synthesis of Amino Acid Cofactor in Cysteine Dioxygenase Is Regulated by Substrate and Represents a Novel Post-translational Regulation of Activity Dominy, John E.; Hwang, Jesse; Guo, Stephanie Journal of Biological Chemistry, Vol. 283, Issue 18 https://doi.org/10.1074/jbc.M800044200	journal	February 2008
Metabolic biomarkers of increased oxidative stress and impaired methylation capacity in children with autism James, S. Jill; Cutler, Paul; Melnyk, Stepan The American Journal of Clinical Nutrition, Vol. 80, Issue 6 https://doi.org/10.1093/ajcn/80.6.1611	journal	December 2004
Density-functional approximation for the correlation energy of the inhomogeneous electron gas Perdew, John P. Physical Review B, Vol. 33, Issue 12 https://doi.org/10.1103/PhysRevB.33.8822	journal	June 1986
Phaser crystallographic software McCoy, Airlie J.; Grosse-Kunstleve, Ralf W.; Adams, Paul D. Journal of Applied Crystallography, Vol. 40, Issue 4 https://doi.org/10.1107/S0021889807021206	journal	July 2007
A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning Padilla, Jennifer E.; Yeates, Todd O. Acta Crystallographica Section D Biological Crystallography, Vol. 59, Issue 7 https://doi.org/10.1107/S0907444903007947	journal	June 2003
Intensity statistics in twinned crystals with examples from the PDB Lebedev, Andrey A.; Vagin, Alexei A.; Murshudov, Garib N. Acta Crystallographica Section D Biological Crystallography, Vol. 62, Issue 1 https://doi.org/10.1107/S0907444905036759	journal	December 2005
Surprises and pitfalls arising from (pseudo)symmetry Zwart, Peter H.; Grosse-Kunstleve, Ralf W.; Lebedev, Andrey A. Acta Crystallographica Section D Biological Crystallography, Vol. 64, Issue 1 https://doi.org/10.1107/S090744490705531X	journal	December 2007
XDS Kabsch, Wolfgang Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2 https://doi.org/10.1107/S0907444909047337	journal	January 2010
Detection and correction of underassigned rotational symmetry prior to structure deposition Poon, Billy K.; Grosse-Kunstleve, Ralf W.; Zwart, Peter H. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 5 https://doi.org/10.1107/S0907444910001502	journal	April 2010
Features and development of Coot Emsley, P.; Lohkamp, B.; Scott, W. G. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 4 https://doi.org/10.1107/S0907444910007493	journal	March 2010
REFMAC 5 for the refinement of macromolecular crystal structures Murshudov, Garib N.; Skubák, Pavol; Lebedev, Andrey A. Acta Crystallographica Section D Biological Crystallography, Vol. 67, Issue 4 https://doi.org/10.1107/S0907444911001314	journal	March 2011
Space-group and origin ambiguity in macromolecular structures with pseudo-symmetry and its treatment with the program Zanuda Lebedev, Andrey A.; Isupov, Michail N. Acta Crystallographica Section D Biological Crystallography, Vol. 70, Issue 9 https://doi.org/10.1107/S1399004714014795	journal	August 2014
Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants Masson, Norma; Keeley, Thomas P.; Giuntoli, Beatrice Science, Vol. 365, Issue 6448 https://doi.org/10.1126/science.aaw0112	journal	July 2019
Identification and Characterization of Bacterial Cysteine Dioxygenases: a New Route of Cysteine Degradation for Eubacteria Dominy, John E.; Simmons, Chad R.; Karplus, P. Andrew Journal of Bacteriology, Vol. 188, Issue 15 https://doi.org/10.1128/JB.00291-06	journal	August 2006
SULFUR AMINO ACID METABOLISM: Pathways for Production and Removal of Homocysteine and Cysteine Stipanuk, Martha H. Annual Review of Nutrition, Vol. 24, Issue 1 https://doi.org/10.1146/annurev.nutr.24.012003.132418	journal	July 2004
Production of 3-Hydroxypropanoic Acid From Glycerol by Metabolically Engineered Bacteria Jers, Carsten; Kalantari, Aida; Garg, Abhroop Frontiers in Bioengineering and Biotechnology, Vol. 7 https://doi.org/10.3389/fbioe.2019.00124	journal	May 2019

Similar Records

Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs: Arg- and Gln-type Bacterial CDO Homologs

Journal Article · Wed Dec 31 19:00:00 EST 2014 · Protein Science · OSTI ID:1179449

Probes of the Catalytic Site of Cysteine Dioxygenase

Journal Article · Sat Dec 31 23:00:00 EST 2005 · Journal of Biological Chemistry · OSTI ID:959577

Spectroscopic and Electronic Structure Study of ETHE1: Elucidating the Factors Influencing Sulfur Oxidation and Oxygenation in Mononuclear Nonheme Iron Enzymes

Journal Article · Mon Oct 15 20:00:00 EDT 2018 · Journal of the American Chemical Society · OSTI ID:1490961

Related Subjects

36 MATERIALS SCIENCE

Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center

Citation Formats

References (88)

Similar Records

Related Subjects