The Mononuclear Molybdenum Enzymes†
Note: In lieu of an abstract, this is the article's first page.
†
This review is dedicated to Professor R. C. Bray in recognition of his 40 years of contribution to the study of molybdenum-containing enzymes.
Cited By
This article is cited by 1390 publications.
- Maiko J. Askari, Jeremy D. Kallick, Charles C. L. McCrory. Selective Reduction of Aqueous Nitrate to Ammonium with an Electropolymerized Chromium Molecular Catalyst. Journal of the American Chemical Society 2024, 146
(11)
, 7439-7455. https://doi.org/10.1021/jacs.3c12783
- Yazdan Maghsoud, Chao Dong, G. Andrés Cisneros. Computational Characterization of the Inhibition Mechanism of Xanthine Oxidoreductase by Topiroxostat. ACS Catalysis 2023, 13
(9)
, 6023-6043. https://doi.org/10.1021/acscatal.3c01245
- Zhenjie Mao, Hong Jiang, Xiangzhao Mao. Identification and Anti-Hyperuricemic Activity of Xanthine Oxidase Inhibitory Peptides from Pacific White Shrimp and Swimming Crab Based on Molecular Docking Screening. Journal of Agricultural and Food Chemistry 2023, 71
(3)
, 1620-1627. https://doi.org/10.1021/acs.jafc.2c07881
- Sven T. Stripp, Benjamin R. Duffus, Vincent Fourmond, Christophe Léger, Silke Leimkühler, Shun Hirota, Yilin Hu, Andrew Jasniewski, Hideaki Ogata, Markus W. Ribbe. Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase. Chemical Reviews 2022, 122
(14)
, 11900-11973. https://doi.org/10.1021/acs.chemrev.1c00914
- Kenichi Yokoyama, Di Li, Haoran Pang. Resolving the Multidecade-Long Mystery in MoaA Radical SAM Enzyme Reveals New Opportunities to Tackle Human Health Problems. ACS Bio & Med Chem Au 2022, 2
(2)
, 94-108. https://doi.org/10.1021/acsbiomedchemau.1c00046
- Mingjie Liu, Azadeh Nazemi, Michael G. Taylor, Aditya Nandy, Chenru Duan, Adam H. Steeves, Heather J. Kulik. Large-Scale Screening Reveals That Geometric Structure Matters More Than Electronic Structure in the Bioinspired Catalyst Design of Formate Dehydrogenase Mimics. ACS Catalysis 2022, 12
(1)
, 383-396. https://doi.org/10.1021/acscatal.1c04624
- Sinan Al-Attar, Julia Rendon, Marlon Sidore, Jean-Pierre Duneau, Farida Seduk, Frédéric Biaso, Stéphane Grimaldi, Bruno Guigliarelli, Axel Magalon. Gating of Substrate Access and Long-Range Proton Transfer in Escherichia coli Nitrate Reductase A: The Essential Role of a Remote Glutamate Residue. ACS Catalysis 2021, 11
(23)
, 14303-14318. https://doi.org/10.1021/acscatal.1c03988
- Janelle Bykowski, Douglas Turnbull, Nolan Hahn, René T. Boeré, Stacey D. Wetmore, Michael Gerken. Lewis Acid Behavior of MoF5 and MoOF4: Syntheses and Characterization of MoF5(NCCH3), MoF5(NC5H5)n, and MoOF4(NC5H5)n (n = 1, 2). Inorganic Chemistry 2021, 60
(20)
, 15695-15711. https://doi.org/10.1021/acs.inorgchem.1c02380
- Jose Lanuza, Ángel Sánchez−González, Nuno A. G. Bandeira, Xabier Lopez, Adrià Gil. Mechanistic Insights into Promoted Hydrolysis of Phosphoester Bonds by MoO2Cl2(DMF)2. Inorganic Chemistry 2021, 60
(15)
, 11177-11191. https://doi.org/10.1021/acs.inorgchem.1c01088
- Mousumi Nayak, Deepak K. Joshi, Krishna Kumar, Anoop S. Singh, Vinod K. Tiwari, Subrato Bhattacharya. Synthesis of a Series of a Few Hydrosulfide Complexes of Cu(I). A μ3-SH-Bridged Rare Cubane-like Tetramer Showing Efficient Catalytic Activity toward Azide–Alkyne Cycloaddition. Inorganic Chemistry 2021, 60
(11)
, 8075-8084. https://doi.org/10.1021/acs.inorgchem.1c00628
- Jenny Y. Yang, Tyler A. Kerr, Xinran S. Wang, Jeffrey M. Barlow. Reducing CO2 to HCO2– at Mild Potentials: Lessons from Formate Dehydrogenase. Journal of the American Chemical Society 2020, 142
(46)
, 19438-19445. https://doi.org/10.1021/jacs.0c07965
- Dibbendu Ghosh, Soumen Sinhababu, Bernard D. Santarsiero, Neal P. Mankad. A W/Cu Synthetic Model for the Mo/Cu Cofactor of Aerobic CODH Indicates That Biochemical CO Oxidation Requires a Frustrated Lewis Acid/Base Pair. Journal of the American Chemical Society 2020, 142
(29)
, 12635-12642. https://doi.org/10.1021/jacs.0c03343
- Haoran Pang, Edward A. Lilla, Pan Zhang, Du Zhang, Thomas P. Shields, Lincoln G. Scott, Weitao Yang, Kenichi Yokoyama. Mechanism of Rate Acceleration of Radical C–C Bond Formation Reaction by a Radical SAM GTP 3′,8-Cyclase. Journal of the American Chemical Society 2020, 142
(20)
, 9314-9326. https://doi.org/10.1021/jacs.0c01200
- Benjamin R. Duffus, Peer Schrapers, Nils Schuth, Stefan Mebs, Holger Dau, Silke Leimkühler, Michael Haumann. Anion Binding and Oxidative Modification at the Molybdenum Cofactor of Formate Dehydrogenase from Rhodobacter capsulatus Studied by X-ray Absorption Spectroscopy. Inorganic Chemistry 2020, 59
(1)
, 214-225. https://doi.org/10.1021/acs.inorgchem.9b01613
- Eirini Armakola, Inés R. Salcedo, Montse Bazaga-García, Pascual Olivera-Pastor, Gellert Mezei, Aurelio Cabeza, Tiago A. Fernandes, Alexander M. Kirillov, Konstantinos D. Demadis. Phosphonate Decomposition-Induced Polyoxomolybdate Dumbbell-Type Cluster Formation: Structural Analysis, Proton Conduction, and Catalytic Sulfoxide Reduction. Inorganic Chemistry 2019, 58
(17)
, 11522-11533. https://doi.org/10.1021/acs.inorgchem.9b01376
- Jing Tang, Rebecka Maria Larsen Werchmeister, Loredana Preda, Wei Huang, Zhiyong Zheng, Silke Leimkühler, Ulla Wollenberger, Xinxin Xiao, Christian Engelbrekt, Jens Ulstrup, Jingdong Zhang. Three-Dimensional Sulfite Oxidase Bioanodes Based on Graphene Functionalized Carbon Paper for Sulfite/O2 Biofuel Cells. ACS Catalysis 2019, 9
(7)
, 6543-6554. https://doi.org/10.1021/acscatal.9b01715
- Stefan Reschke, Benjamin R. Duffus, Peer Schrapers, Stefan Mebs, Christian Teutloff, Holger Dau, Michael Haumann, Silke Leimkühler. Identification of YdhV as the First Molybdoenzyme Binding a Bis-Mo-MPT Cofactor in Escherichia coli. Biochemistry 2019, 58
(17)
, 2228-2242. https://doi.org/10.1021/acs.biochem.9b00078
- Paul Kaufmann, Benjamin R. Duffus, Christian Teutloff, Silke Leimkühler. Functional Studies on Oligotropha carboxidovorans Molybdenum–Copper CO Dehydrogenase Produced in Escherichia coli. Biochemistry 2018, 57
(19)
, 2889-2901. https://doi.org/10.1021/acs.biochem.8b00128
- Lee Taylor Elrod, Eunsuk Kim. Lewis Acid Assisted Nitrate Reduction with Biomimetic Molybdenum Oxotransferase Complex. Inorganic Chemistry 2018, 57
(5)
, 2594-2602. https://doi.org/10.1021/acs.inorgchem.7b02956
- Paul Kaufmann, Benjamin R. Duffus, Biljana Mitrova, Chantal Iobbi-Nivol, Christian Teutloff, Manfred Nimtz, Lothar Jänsch, Ulla Wollenberger, and Silke Leimkühler . Modulating the Molybdenum Coordination Sphere of Escherichia coli Trimethylamine N-Oxide Reductase. Biochemistry 2018, 57
(7)
, 1130-1143. https://doi.org/10.1021/acs.biochem.7b01108
- Sebastian Gohr, Peter Hrobárik, and Martin Kaupp . Four-Component Relativistic Density Functional Calculations of EPR Parameters for Model Complexes of Tungstoenzymes. The Journal of Physical Chemistry A 2017, 121
(47)
, 9106-9117. https://doi.org/10.1021/acs.jpca.7b08768
- Sudarshana Majumder, Sagarika Pasayat, Alok K. Panda, Subhashree P. Dash, Satabdi Roy, Ashis Biswas, Mokshada E. Varma, Bimba N. Joshi, Eugenio Garribba, Chahat Kausar, Samir Kumar Patra, Werner Kaminsky, Aurélien Crochet, and Rupam Dinda . Monomeric and Dimeric Oxidomolybdenum(V and VI) Complexes, Cytotoxicity, and DNA Interaction Studies: Molybdenum Assisted C═N Bond Cleavage of Salophen Ligands. Inorganic Chemistry 2017, 56
(18)
, 11190-11210. https://doi.org/10.1021/acs.inorgchem.7b01578
- Chao Dong, Jing Yang, Stefan Reschke, Silke Leimkühler, and Martin L. Kirk . Vibrational Probes of Molybdenum Cofactor–Protein Interactions in Xanthine Dehydrogenase. Inorganic Chemistry 2017, 56
(12)
, 6830-6837. https://doi.org/10.1021/acs.inorgchem.7b00028
- Stefan Reschke, Stefan Mebs, Kajsa G. V. Sigfridsson-Clauss, Ramona Kositzki, Silke Leimkühler, and Michael Haumann . Protonation and Sulfido versus Oxo Ligation Changes at the Molybdenum Cofactor in Xanthine Dehydrogenase (XDH) Variants Studied by X-ray Absorption Spectroscopy. Inorganic Chemistry 2017, 56
(4)
, 2165-2176. https://doi.org/10.1021/acs.inorgchem.6b02846
- Pengfei Li and Kenneth M. Merz, Jr. . Metal Ion Modeling Using Classical Mechanics. Chemical Reviews 2017, 117
(3)
, 1564-1686. https://doi.org/10.1021/acs.chemrev.6b00440
- Aurélien B. Ducrot, Ben A. Coulson, Robin N. Perutz, and Anne-Kathrin Duhme-Klair . Light-Induced Activation of a Molybdenum Oxotransferase Model within a Ru(II)–Mo(VI) Dyad. Inorganic Chemistry 2016, 55
(24)
, 12583-12594. https://doi.org/10.1021/acs.inorgchem.6b01485
- Lorenzo Fernández, Francisco F. Pérez-Pla, Iñaki Tuñón, and Elisa Llopis . DFT Study on the Interaction of Tris(benzene-1,2-dithiolato)molybdenum Complex with Water. A Hydrolysis Mechanism Involving a Feasible Seven-Coordinate Aquomolybdenum Intermediate. The Journal of Physical Chemistry A 2016, 120
(48)
, 9636-9646. https://doi.org/10.1021/acs.jpca.6b10233
- Márcia A. S. Correia, Ana Rita Otrelo-Cardoso, Viola Schwuchow, Kajsa G. V. Sigfridsson Clauss, Michael Haumann, Maria João Romão, Silke Leimkühler, and Teresa Santos-Silva . The Escherichia coli Periplasmic Aldehyde Oxidoreductase Is an Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes. ACS Chemical Biology 2016, 11
(10)
, 2923-2935. https://doi.org/10.1021/acschembio.6b00572
- David Sarauli, Anja Borowski, Kristina Peters, Burkhard Schulz, Dina Fattakhova-Rohlfing, Silke Leimkühler, and Fred Lisdat . Investigation of the pH-Dependent Impact of Sulfonated Polyaniline on Bioelectrocatalytic Activity of Xanthine Dehydrogenase. ACS Catalysis 2016, 6
(10)
, 7152-7159. https://doi.org/10.1021/acscatal.6b02011
- Hiroumi Mitome, Tomoya Ishizuka, Hiroaki Kotani, Yoshihito Shiota, Kazunari Yoshizawa, and Takahiko Kojima . Mechanistic Insights into C–H Oxidations by Ruthenium(III)-Pterin Complexes: Impact of Basicity of the Pterin Ligand and Electron Acceptability of the Metal Center on the Transition States. Journal of the American Chemical Society 2016, 138
(30)
, 9508-9520. https://doi.org/10.1021/jacs.6b03785
- Luisa B. Maia, Luis Fonseca, Isabel Moura, and José J. G. Moura . Reduction of Carbon Dioxide by a Molybdenum-Containing Formate Dehydrogenase: A Kinetic and Mechanistic Study. Journal of the American Chemical Society 2016, 138
(28)
, 8834-8846. https://doi.org/10.1021/jacs.6b03941
- Chloe Westley, Yun Xu, Andrew J. Carnell, Nicholas J. Turner, and Royston Goodacre . Label-Free Surface Enhanced Raman Scattering Approach for High-Throughput Screening of Biocatalysts. Analytical Chemistry 2016, 88
(11)
, 5898-5903. https://doi.org/10.1021/acs.analchem.6b00813
- Tobias Hartmann, Peer Schrapers, Tillmann Utesch, Manfred Nimtz, Yvonne Rippers, Holger Dau, Maria Andrea Mroginski, Michael Haumann, and Silke Leimkühler . The Molybdenum Active Site of Formate Dehydrogenase Is Capable of Catalyzing C–H Bond Cleavage and Oxygen Atom Transfer Reactions. Biochemistry 2016, 55
(16)
, 2381-2389. https://doi.org/10.1021/acs.biochem.6b00002
- Lianrui Hu and Hui Chen . Assessment of DFT Methods for Computing Activation Energies of Mo/W-Mediated Reactions. Journal of Chemical Theory and Computation 2015, 11
(10)
, 4601-4614. https://doi.org/10.1021/acs.jctc.5b00373
- Loredana Brinza, Hong P. Vu, Samuel Shaw, J. Fred W. Mosselmans, and Liane G. Benning . Effect of Mo and V on the Hydrothermal Crystallization of Hematite from Ferrihydrite: An in Situ Energy Dispersive X-ray Diffraction and X-ray Absorption Spectroscopy Study. Crystal Growth & Design 2015, 15
(10)
, 4768-4780. https://doi.org/10.1021/acs.cgd.5b00173
- Ting Zeng, Silke Leimkühler, Joachim Koetz, and Ulla Wollenberger . Effective Electrochemistry of Human Sulfite Oxidase Immobilized on Quantum-Dots-Modified Indium Tin Oxide Electrode. ACS Applied Materials & Interfaces 2015, 7
(38)
, 21487-21494. https://doi.org/10.1021/acsami.5b06665
- Peer Schrapers, Tobias Hartmann, Ramona Kositzki, Holger Dau, Stefan Reschke, Carola Schulzke, Silke Leimkühler, and Michael Haumann . Sulfido and Cysteine Ligation Changes at the Molybdenum Cofactor during Substrate Conversion by Formate Dehydrogenase (FDH) from Rhodobacter capsulatus. Inorganic Chemistry 2015, 54
(7)
, 3260-3271. https://doi.org/10.1021/ic502880y
- Palraj Kalimuthu, Johann Heider, Daniel Knack, and Paul V. Bernhardt . Electrocatalytic Hydrocarbon Hydroxylation by Ethylbenzene Dehydrogenase from Aromatoleum aromaticum. The Journal of Physical Chemistry B 2015, 119
(8)
, 3456-3463. https://doi.org/10.1021/jp512562k
- Luisa B. Maia, Vânia Pereira, Lurdes Mira, and José J. G. Moura . Nitrite Reductase Activity of Rat and Human Xanthine Oxidase, Xanthine Dehydrogenase, and Aldehyde Oxidase: Evaluation of Their Contribution to NO Formation in Vivo. Biochemistry 2015, 54
(3)
, 685-710. https://doi.org/10.1021/bi500987w
- Wei Zhao, Patrick K. Yan, and Alexander T. Radosevich . A Phosphetane Catalyzes Deoxygenative Condensation of α-Keto Esters and Carboxylic Acids via PIII/PV═O Redox Cycling. Journal of the American Chemical Society 2015, 137
(2)
, 616-619. https://doi.org/10.1021/ja511889y
- Jana Leppin, Christoph Förster, and Katja Heinze . Molybdenum Complex with Bulky Chelates as a Functional Model for Molybdenum Oxidases. Inorganic Chemistry 2014, 53
(23)
, 12416-12427. https://doi.org/10.1021/ic501751p
- Jilai Li and Ulf Ryde . Comparison of the Active-Site Design of Molybdenum Oxo-Transfer Enzymes by Quantum Mechanical Calculations. Inorganic Chemistry 2014, 53
(22)
, 11913-11924. https://doi.org/10.1021/ic5010837
- Hongnan Cao, James M. Pauff, and Russ Hille . X-ray Crystal Structure of a Xanthine Oxidase Complex with the Flavonoid Inhibitor Quercetin. Journal of Natural Products 2014, 77
(7)
, 1693-1699. https://doi.org/10.1021/np500320g
- Michael J. van Stipdonk, Partha Basu, Sara A. Dille, John K. Gibson, Giel Berden, and Jos Oomens . Infrared Multiple Photon Dissociation Spectroscopy of a Gas-Phase Oxo-Molybdenum Complex with 1,2-Dithiolene Ligands. The Journal of Physical Chemistry A 2014, 118
(29)
, 5407-5418. https://doi.org/10.1021/jp503222v
- B. Zhang, X. M. Lu, K. Li, S. Z. Du, G. Wang, and Q. Wang . Improving and Fining of Nanostructures by Mixing W with Mo in Metal Organic Hybrid Crystal. Crystal Growth & Design 2014, 14
(7)
, 3249-3256. https://doi.org/10.1021/cg401839m
- Aaron Hahn, Stefan Reschke, Silke Leimkühler, and Thomas Risse . Ketoxime Coupling of p-Acetylphenylalanine at Neutral pH for Site-Directed Spin Labeling of Human Sulfite Oxidase. The Journal of Physical Chemistry B 2014, 118
(25)
, 7077-7084. https://doi.org/10.1021/jp503471j
- Yang Ha, Adam L. Tenderholt, Richard H. Holm, Britt Hedman, Keith O. Hodgson, and Edward I. Solomon . Sulfur K-Edge X-ray Absorption Spectroscopy and Density Functional Theory Calculations on Monooxo MoIV and Bisoxo MoVI Bis-dithiolenes: Insights into the Mechanism of Oxo Transfer in Sulfite Oxidase and Its Relation to the Mechanism of DMSO Reductase. Journal of the American Chemical Society 2014, 136
(25)
, 9094-9105. https://doi.org/10.1021/ja503316p
- Luisa B. Maia and José J. G. Moura . How Biology Handles Nitrite. Chemical Reviews 2014, 114
(10)
, 5273-5357. https://doi.org/10.1021/cr400518y
- Jing Liu, Saumen Chakraborty, Parisa Hosseinzadeh, Yang Yu, Shiliang Tian, Igor Petrik, Ambika Bhagi, and Yi Lu . Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers. Chemical Reviews 2014, 114
(8)
, 4366-4469. https://doi.org/10.1021/cr400479b
- Margareta R. A. Blomberg, Tomasz Borowski, Fahmi Himo, Rong-Zhen Liao, and Per E. M. Siegbahn . Quantum Chemical Studies of Mechanisms for Metalloenzymes. Chemical Reviews 2014, 114
(7)
, 3601-3658. https://doi.org/10.1021/cr400388t
- Russ Hille, James Hall, and Partha Basu . The Mononuclear Molybdenum Enzymes. Chemical Reviews 2014, 114
(7)
, 3963-4038. https://doi.org/10.1021/cr400443z
- Hongnan Cao, James Hall, and Russ Hille . Substrate Orientation and Specificity in Xanthine Oxidase: Crystal Structures of the Enzyme in Complex with Indole-3-acetaldehyde and Guanine. Biochemistry 2014, 53
(3)
, 533-541. https://doi.org/10.1021/bi401465u
- Muralidharan Shanmugam, Jarett Wilcoxen, Diana Habel-Rodriguez, George E. Cutsail III, Martin L. Kirk, Brian M. Hoffman, and Russ Hille . 13C and 63,65Cu ENDOR studies of CO Dehydrogenase from Oligotropha carboxidovorans. Experimental Evidence in Support of a Copper–Carbonyl Intermediate. Journal of the American Chemical Society 2013, 135
(47)
, 17775-17782. https://doi.org/10.1021/ja406136f
- Stefan Reschke, Dimitri Niks, Heather Wilson, Kajsa G. V. Sigfridsson, Michael Haumann, K. V. Rajagopalan, Russ Hille, and Silke Leimkühler . Effect of Exchange of the Cysteine Molybdenum Ligand with Selenocysteine on the Structure and Function of the Active Site in Human Sulfite Oxidase. Biochemistry 2013, 52
(46)
, 8295-8303. https://doi.org/10.1021/bi4008512
- Nuno M. F. S. A. Cerqueira, Pedro A. Fernandes, Pablo J. Gonzalez, José J. G. Moura, and Maria J. Ramos . The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase. Inorganic Chemistry 2013, 52
(19)
, 10766-10772. https://doi.org/10.1021/ic3028034
- Junhyeok Seo, Paul G. Williard, and Eunsuk Kim . Deoxygenation of Mono-oxo Bis(dithiolene) Mo and W Complexes by Protonation. Inorganic Chemistry 2013, 52
(15)
, 8706-8712. https://doi.org/10.1021/ic4008747
- Palraj Kalimuthu, Katrin Fischer-Schrader, Günter Schwarz, and Paul V. Bernhardt . Mediated Electrochemistry of Nitrate Reductase from Arabidopsis thaliana. The Journal of Physical Chemistry B 2013, 117
(25)
, 7569-7577. https://doi.org/10.1021/jp404076w
- Bradley M. Hover, Anna Loksztejn, Anthony A. Ribeiro, and Kenichi Yokoyama . Identification of a Cyclic Nucleotide as a Cryptic Intermediate in Molybdenum Cofactor Biosynthesis. Journal of the American Chemical Society 2013, 135
(18)
, 7019-7032. https://doi.org/10.1021/ja401781t
- Golam Moula, Moumita Bose, and Sabyasachi Sarkar . Replica of a Fishy Enzyme: Structure–Function Analogue of Trimethylamine-N-Oxide Reductase. Inorganic Chemistry 2013, 52
(9)
, 5316-5327. https://doi.org/10.1021/ic4002576
- Joyee Mitra and Sabyasachi Sarkar . Oxo–Mo(IV)(dithiolene)thiolato Complexes: Analogue of Reduced Sulfite Oxidase. Inorganic Chemistry 2013, 52
(6)
, 3032-3042. https://doi.org/10.1021/ic302485c
- Ji-Lai Li, Ricardo A. Mata, and Ulf Ryde . Large Density-Functional and Basis-Set Effects for the DMSO Reductase Catalyzed Oxo-Transfer Reaction. Journal of Chemical Theory and Computation 2013, 9
(3)
, 1799-1807. https://doi.org/10.1021/ct301094r
- Marios Stylianou, Vladimiros A. Nikolakis, George I. Chilas, Tamas Jakusch, Tiverios Vaimakis, Tamas Kiss, Michael P. Sigalas, Anastasios D. Keramidas, and Themistoklis A. Kabanos . Molybdenum(VI) Coordination Chemistry of the N,N-Disubstituted Bis(hydroxylamido)-1,3,5-triazine Ligand, H2bihyat. Water-Assisted Activation of the MoVI═O Bond and Reversible Dimerization of cis-[MoVIO2(bihyat)] to [MoVI2O4(bihyat)2(H2O)2]. Inorganic Chemistry 2012, 51
(24)
, 13138-13147. https://doi.org/10.1021/ic301282q
- Palraj Kalimuthu, Silke Leimkühler, and Paul V. Bernhardt . Low-Potential Amperometric Enzyme Biosensor for Xanthine and Hypoxanthine. Analytical Chemistry 2012, 84
(23)
, 10359-10365. https://doi.org/10.1021/ac3025027
- Palraj Kalimuthu, Silke Leimkühler, and Paul V. Bernhardt . Catalytic Electrochemistry of Xanthine Dehydrogenase. The Journal of Physical Chemistry B 2012, 116
(38)
, 11600-11607. https://doi.org/10.1021/jp307374z
- Junhyeok Seo and Eunsuk Kim . O-Atom Exchange between H2O and CO2 Mediated by a Bis(dithiolene)tungsten Complex. Inorganic Chemistry 2012, 51
(15)
, 7951-7953. https://doi.org/10.1021/ic300906j
- Mohammad Amin Mir, Javed Masood Khan, Rizwan Hasan Khan, Aijaz Ahmad Dar, and Ghulam Mohammad Rather . Interaction of Cetyltrimethylammonium Bromide and Its Gemini Homologue Bis(cetyldimethylammonium)butane Dibromide with Xanthine Oxidase. The Journal of Physical Chemistry B 2012, 116
(19)
, 5711-5718. https://doi.org/10.1021/jp207803c
- Tapan K. Kundu, Murugesan Velayutham, and Jay L. Zweier . Aldehyde Oxidase Functions as a Superoxide Generating NADH Oxidase: An Important Redox Regulated Pathway of Cellular Oxygen Radical Formation. Biochemistry 2012, 51
(13)
, 2930-2939. https://doi.org/10.1021/bi3000879
- Tillmann Utesch, Murat Sezer, Inez M. Weidinger, and Maria Andrea Mroginski . Adsorption of Sulfite Oxidase on Self-Assembled Monolayers from Molecular Dynamics Simulations. Langmuir 2012, 28
(13)
, 5761-5769. https://doi.org/10.1021/la205055g
- Kristina Hüttinger, Christoph Förster, Timo Bund, Dariush Hinderberger, and Katja Heinze . Stereochemical Consequences of Oxygen Atom Transfer and Electron Transfer in Imido/Oxido Molybdenum(IV, V, VI) Complexes with Two Unsymmetric Bidentate Ligands. Inorganic Chemistry 2012, 51
(7)
, 4180-4192. https://doi.org/10.1021/ic202588u
- Frédéric Biaso, Bénédicte Burlat, and Bruno Guigliarelli . DFT Investigation of the Molybdenum Cofactor in Periplasmic Nitrate Reductases: Structure of the Mo(V) EPR-Active Species. Inorganic Chemistry 2012, 51
(6)
, 3409-3419. https://doi.org/10.1021/ic201533p
- Adam L. Tenderholt, Keith O. Hodgson, Britt Hedman, Richard H. Holm, and Edward I. Solomon . Substrate and Metal Control of Barrier Heights for Oxo Transfer to Mo and W Bis-dithiolene Sites. Inorganic Chemistry 2012, 51
(6)
, 3436-3442. https://doi.org/10.1021/ic2020397
- Andrei V. Astashkin, Asha Rajapakshe, Matthew J. Cornelison, Kayunta Johnson-Winters, and John H. Enemark . Determination of the Distance between the Mo(V) and Fe(III) Heme Centers of Wild Type Human Sulfite Oxidase by Pulsed EPR Spectroscopy. The Journal of Physical Chemistry B 2012, 116
(6)
, 1942-1950. https://doi.org/10.1021/jp210578f
- Eric L. Klein, Arnold M. Raitsimring, Andrei V. Astashkin, Asha Rajapakshe, Kayunta Johnson-Winters, Anna R. Arnold, Alexey Potapov, Daniella Goldfarb, and John H. Enemark . Identity of the Exchangeable Sulfur-Containing Ligand at the Mo(V) Center of R160Q Human Sulfite Oxidase. Inorganic Chemistry 2012, 51
(3)
, 1408-1418. https://doi.org/10.1021/ic201643t
- Manuel Volpe and Nadia C. Mösch-Zanetti . Molybdenum(VI) Dioxo and Oxo-Imido Complexes of Fluorinated β-Ketiminato Ligands and Their Use in OAT Reactions. Inorganic Chemistry 2012, 51
(3)
, 1440-1449. https://doi.org/10.1021/ic201681u
- Hiroshi Ishikita, Bryan T. Eger, Ken Okamoto, Takeshi Nishino, and Emil F. Pai . Protein Conformational Gating of Enzymatic Activity in Xanthine Oxidoreductase. Journal of the American Chemical Society 2012, 134
(2)
, 999-1009. https://doi.org/10.1021/ja207173p
- T. Arumuganathan, Manuel Volpe, Bastian Harum, Dietmar Wurm, Ferdinand Belaj, and Nadia C. Mösch-Zanetti . Unusual Nonoctahedral Geometry with Molybdenum Oxoimido Complexes Containing η2-Pyrazolate Ligands. Inorganic Chemistry 2012, 51
(1)
, 150-156. https://doi.org/10.1021/ic201308g
- Joseph Sempombe, Benjamin Stein, and Martin L. Kirk . Spectroscopic and Electronic Structure Studies Probing Covalency Contributions to C–H Bond Activation and Transition-State Stabilization in Xanthine Oxidase. Inorganic Chemistry 2011, 50
(21)
, 10919-10928. https://doi.org/10.1021/ic201477n
- Asha Rajapakshe, Andrei V. Astashkin, Eric L. Klein, Debora Reichmann, Ralf R. Mendel, Florian Bittner, and John H. Enemark . Structural Studies of the Molybdenum Center of Mitochondrial Amidoxime Reducing Component (mARC) by Pulsed EPR Spectroscopy and 17O-Labeling. Biochemistry 2011, 50
(41)
, 8813-8822. https://doi.org/10.1021/bi2005762
- Jeremiah J. Scepaniak, Charles G. Margarit, Jeremy N. Harvey, and Jeremy M. Smith . Nitrogen Atom Transfer from Iron(IV) Nitrido Complexes: A Dual-Nature Transition State for Atom Transfer. Inorganic Chemistry 2011, 50
(19)
, 9508-9517. https://doi.org/10.1021/ic201190c
- Hongnan Cao, James Hall, and Russ Hille . X-ray Crystal Structure of Arsenite-Inhibited Xanthine Oxidase: μ-Sulfido,μ-Oxo Double Bridge between Molybdenum and Arsenic in the Active Site. Journal of the American Chemical Society 2011, 133
(32)
, 12414-12417. https://doi.org/10.1021/ja2050265
- Hanit Marom, Svetlana Antonov, Yanay Popowski, and Michael Gozin . Selective Sulfoxidation of Thioethers and Thioaryl Boranes with Nitrate, Promoted by a Molybdenum–Copper Catalytic System. The Journal of Organic Chemistry 2011, 76
(13)
, 5240-5246. https://doi.org/10.1021/jo2001808
- Regina P. Mtei, Ganna Lyashenko, Benjamin Stein, Nick Rubie, Russ Hille, and Martin L. Kirk . Spectroscopic and Electronic Structure Studies of a Dimethyl Sulfoxide Reductase Catalytic Intermediate: Implications for Electron- and Atom-Transfer Reactivity. Journal of the American Chemical Society 2011, 133
(25)
, 9762-9774. https://doi.org/10.1021/ja109178q
- Stephen Sproules, Aston A. Eagle, Michelle K. Taylor, Robert W. Gable, Jonathan M. White, and Charles G. Young . Paramagnetic Oxotungsten(V) Complexes Containing the Hydrotris(3,5-dimethylpyrazol-1-yl)borate Ligand. Inorganic Chemistry 2011, 50
(10)
, 4503-4514. https://doi.org/10.1021/ic200161m
- Palraj Kalimuthu, Silke Leimkühler, and Paul V. Bernhardt . Xanthine Dehydrogenase Electrocatalysis: Autocatalysis and Novel Activity. The Journal of Physical Chemistry B 2011, 115
(11)
, 2655-2662. https://doi.org/10.1021/jp111809f
- Jarett Wilcoxen, Bo Zhang, and Russ Hille . Reaction of the Molybdenum- and Copper-Containing Carbon Monoxide Dehydrogenase from Oligotropha carboxydovorans with Quinones. Biochemistry 2011, 50
(11)
, 1910-1916. https://doi.org/10.1021/bi1017182
- M. Jake Pushie, Christian J. Doonan, Kamila Moquin, Joel H. Weiner, Richard Rothery, and Graham N. George . Molybdenum Site Structure of Escherichia coli YedY, a Novel Bacterial Oxidoreductase. Inorganic Chemistry 2011, 50
(3)
, 732-740. https://doi.org/10.1021/ic101280m
- Kajsa G. V. Havelius, Stefan Reschke, Sebastian Horn, Alexander Döring, Dimitri Niks, Russ Hille, Carola Schulzke, Silke Leimkühler, and Michael Haumann . Structure of the Molybdenum Site in YedY, a Sulfite Oxidase Homologue from Escherichia coli. Inorganic Chemistry 2011, 50
(3)
, 741-748. https://doi.org/10.1021/ic101291j
- Joseph Essilfie-Dughan, Ingrid J. Pickering, M. Jim Hendry, Graham N. George, and Tom Kotzer . Molybdenum Speciation in Uranium Mine Tailings Using X-Ray Absorption Spectroscopy. Environmental Science & Technology 2011, 45
(2)
, 455-460. https://doi.org/10.1021/es102954b
- Ken Okamoto, Yuko Kawaguchi, Bryan T. Eger, Emil F. Pai, and Takeshi Nishino . Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate. Journal of the American Chemical Society 2010, 132
(48)
, 17080-17083. https://doi.org/10.1021/ja1077574
- Tillmann Utesch and Maria Andrea Mroginski. Three-Dimensional Structural Model of Chicken Liver Sulfite Oxidase in its Activated Form. The Journal of Physical Chemistry Letters 2010, 1
(23)
, 2159-2164. https://doi.org/10.1021/jz1005847
- Victor W. L. Ng, Michelle K. Taylor, Jonathan M. White, and Charles G. Young . cis-Dioxo- and cis-(Hydroxo)oxo-Mo(V) Complexes Stabilized by Intramolecular Hydrogen-Bonding. Inorganic Chemistry 2010, 49
(20)
, 9460-9469. https://doi.org/10.1021/ic1011428
- Muralidharan Shanmugam, Bo Zhang, Rebecca L. McNaughton, R. Adam Kinney, Russ Hille, and Brian M. Hoffman . The Structure of Formaldehyde-Inhibited Xanthine Oxidase Determined by 35 GHz 2H ENDOR Spectroscopy. Journal of the American Chemical Society 2010, 132
(40)
, 14015-14017. https://doi.org/10.1021/ja106432h
- Nadia C. Mösch-Zanetti, Dietmar Wurm, Manuel Volpe, Ganna Lyashenko, Bastian Harum, Ferdinand Belaj, and Judith Baumgartner . Replacement of an Oxo by an Imido Group in Oxotransferase Model Compounds: Influence on the Oxygen Atom Transfer. Inorganic Chemistry 2010, 49
(19)
, 8914-8921. https://doi.org/10.1021/ic101159g
- Eugene T. McGuinness. Some Molecular Moments of the Hadean and Archaean Aeons: A Retrospective Overview from the Interfacing Years of the Second to Third Millennia. Chemical Reviews 2010, 110
(9)
, 5191-5215. https://doi.org/10.1021/cr050061l
- Rosa Llusar, Victor Polo, Ederley Velez and Cristian Vicent . Sulfur-Based Redox Reactions in Mo3S74+ and Mo3S44+ Clusters Bearing Halide and 1,2-Dithiolene Ligands: a Mass Spectrometric and Density Functional Theory Study. Inorganic Chemistry 2010, 49
(17)
, 8045-8055. https://doi.org/10.1021/ic1010693
- Palraj Kalimuthu, Jan Tkac, Ulrike Kappler, Jason J. Davis and Paul V. Bernhardt. Highly Sensitive and Stable Electrochemical Sulfite Biosensor Incorporating a Bacterial Sulfite Dehydrogenase. Analytical Chemistry 2010, 82
(17)
, 7374-7379. https://doi.org/10.1021/ac101493y
- Kayunta Johnson-Winters, Gordon Tollin and John H. Enemark. Elucidating the Catalytic Mechanism of Sulfite Oxidizing Enzymes Using Structural, Spectroscopic, and Kinetic Analyses. Biochemistry 2010, 49
(34)
, 7242-7254. https://doi.org/10.1021/bi1008485
- Asha Rajapakshe, Kayunta Johnson-Winters, Anna R. Nordstrom, Kimberly T. Meyers, Safia Emesh, Andrei V. Astashkin and John H. Enemark. Characterization of Chloride-Depleted Human Sulfite Oxidase by Electron Paramagnetic Resonance Spectroscopy: Experimental Evidence for the Role of Anions in Product Release. Biochemistry 2010, 49
(25)
, 5154-5159. https://doi.org/10.1021/bi902172n
- Adam L. Tenderholt, Jun-Jieh Wang, Robert K. Szilagyi, Richard H. Holm, Keith O. Hodgson, Britt Hedman and Edward I. Solomon. Sulfur K-Edge X-ray Absorption Spectroscopy and Density Functional Calculations on Mo(IV) and Mo(VI)═O Bis-dithiolenes: Insights into the Mechanism of Oxo Transfer in DMSO Reductase and Related Functional Analogues. Journal of the American Chemical Society 2010, 132
(24)
, 8359-8371. https://doi.org/10.1021/ja910369c
- Hideki Sugimoto, Susumu Tatemoto, Koichiro Suyama, Hiroyuki Miyake, Regina P. Mtei, Shinobu Itoh and Martin L. Kirk . Monooxomolybdenum(VI) Complexes Possessing Olefinic Dithiolene Ligands: Probing Mo−S Covalency Contributions to Electron Transfer in Dimethyl Sulfoxide Reductase Family Molybdoenzymes. Inorganic Chemistry 2010, 49
(12)
, 5368-5370. https://doi.org/10.1021/ic100825x