| 1 | Structural and Mechanistic Advances in the Chemistry of Methyl-Coenzyme M Reductase (MCR) | 11.6 | 13 | Citations (PDF) |
| 2 | Nature-Inspired Radical Pyridoxal-Mediated C–C Bond Formation | 11.7 | 16 | Citations (PDF) |
| 3 | S-adenosyl-L-methionine is the unexpected methyl donor for the methylation of mercury by the membrane-associated HgcAB complex | 5.2 | 11 | Citations (PDF) |
| 4 | Characterization of Methyl- and Acetyl-Ni Intermediates in Acetyl CoA Synthase Formed during Anaerobic CO2 and CO Fixation | 11.7 | 25 | Citations (PDF) |
| 5 | Regulation of protein function and degradation by heme, heme responsive motifs, and CO | 3.9 | 21 | Citations (PDF) |
| 6 | Not a “they” but a “we”: The microbiome helps promote our well-being | 1.3 | 4 | Citations (PDF) |
| 7 | Heme oxygenase-2 (HO-2) binds and buffers labile ferric heme in human embryonic kidney cells | 1.3 | 23 | Citations (PDF) |
| 8 | XFEL serial crystallography reveals the room temperature structure of methyl-coenzyme M reductase | 2.3 | 18 | Citations (PDF) |
| 9 | Efficient, Light-Driven Reduction of CO2 to CO by a Carbon Monoxide Dehydrogenase–CdSe/CdS Nanorod Photosystem | 2.9 | 10 | Citations (PDF) |
| 10 | Heme delivery to heme oxygenase-2 involves glyceraldehyde-3-phosphate dehydrogenase | 1.2 | 21 | Citations (PDF) |
| 11 | Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase | 2.4 | 17 | Citations (PDF) |
| 12 | Nickel–Sulfonate Mode of Substrate Binding for Forward and Reverse Reactions of Methyl-SCoM Reductase Suggest a Radical Mechanism Involving Long-Range Electron Transfer | 11.7 | 21 | Citations (PDF) |
| 13 | Ferric heme as a CO/NO sensor in the nuclear receptor Rev-Erbß by coupling gas binding to electron transfer | 5.2 | 35 | Citations (PDF) |
| 14 | Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase | 9.8 | 43 | Citations (PDF) |
| 15 | 13
C Electron Nuclear Double Resonance Spectroscopy Shows Acetyl-CoA Synthase Binds Two Substrate CO in Multiple Binding Modes and Reveals the Importance of a CO-Binding “Alcove” | 11.7 | 15 | Citations (PDF) |
| 16 | Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site | 1.3 | 31 | Citations (PDF) |
| 17 | Structure determination of the HgcAB complex using metagenome sequence data: insights into microbial mercury methylation | 3.1 | 54 | Citations (PDF) |
| 18 | The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation | 1.3 | 23 | Citations (PDF) |
| 19 | Oxygen and Conformation Dependent Protein Oxidation and Aggregation by Porphyrins in Hepatocytes and Light-Exposed Cells | 4.0 | 26 | Citations (PDF) |
| 20 | Kinetics of Enzymatic Mercury Methylation at Nanomolar Concentrations Catalyzed by HgcAB | 2.4 | 32 | Citations (PDF) |
| 21 | Dynamic and structural differences between heme oxygenase-1 and -2 are due to differences in their C-terminal regions | 1.3 | 26 | Citations (PDF) |
| 22 | Fast and Selective Photoreduction of CO2 to CO Catalyzed by a Complex of Carbon Monoxide Dehydrogenase, TiO2, and Ag Nanoclusters | 9.8 | 113 | Citations (PDF) |
| 23 | Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from
Moorella thermoacetica | 5.2 | 34 | Citations (PDF) |
| 24 | Redox Regulation of Heme Oxygenase-2 and the Transcription Factor, Rev-Erb, Through Heme Regulatory Motifs | 4.1 | 30 | Citations (PDF) |
| 25 | An unlikely heme chaperone confirmed at last | 1.3 | 14 | Citations (PDF) |
| 26 | X-ray Absorption Spectroscopy Reveals an Organometallic Ni–C Bond in the CO-Treated Form of Acetyl-CoA Synthase | 1.5 | 36 | Citations (PDF) |
| 27 | Properties of Intermediates in the Catalytic Cycle of Oxalate Oxidoreductase and Its Suicide Inactivation by Pyruvate | 1.5 | 11 | Citations (PDF) |
| 28 | The heme-regulatory motif of nuclear receptor Rev-erbβ is a key mediator of heme and redox signaling in circadian rhythm maintenance and metabolism | 1.3 | 39 | Citations (PDF) |
| 29 | Exploring Hydrogenotrophic Methanogenesis: a Genome Scale Metabolic Reconstruction of Methanococcus maripaludis | 2.2 | 62 | Citations (PDF) |
| 30 | The radical mechanism of biological methane synthesis by methyl-coenzyme M reductase | 26.1 | 168 | Citations (PDF) |
| 31 | Protonation of the Hydroperoxo Intermediate of Cytochrome P450 2B4 Is Slower in the Presence of Cytochrome P450 Reductase Than in the Presence of Cytochrome b5 | 1.5 | 21 | Citations (PDF) |
| 32 | High Affinity Heme Binding to a Heme Regulatory Motif on the Nuclear Receptor Rev-erbβ Leads to Its Degradation and Indirectly Regulates Its Interaction with Nuclear Receptor Corepressor | 1.3 | 48 | Citations (PDF) |
| 33 | One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography | 5.2 | 20 | Citations (PDF) |
| 34 | Comparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases-1 and -2: Kinetic and Cryoreduction Studies | 1.5 | 9 | Citations (PDF) |
| 35 | Investigations by Protein Film Electrochemistry of Alternative Reactions of Nickel-Containing Carbon Monoxide Dehydrogenase | 2.0 | 47 | Citations (PDF) |
| 36 | The C-Terminal Heme Regulatory Motifs of Heme Oxygenase-2 Are Redox-Regulated Heme Binding Sites | 1.5 | 33 | Citations (PDF) |
| 37 | The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism | 1.5 | 22 | Citations (PDF) |
| 38 | Spectroscopic Studies Reveal That the Heme Regulatory Motifs of Heme Oxygenase-2 Are Dynamically Disordered and Exhibit Redox-Dependent Interaction with Heme | 1.5 | 19 | Citations (PDF) |
| 39 | The Reaction Mechanism of Methyl-Coenzyme M Reductase | 1.3 | 66 | Citations (PDF) |
| 40 | Dramatic Conformational Flexibility of Carbon Monoxide Dehydrogenase/Acetyl‐CoA Synthase Revealed by Electron Microscopy | 2.3 | 0 | Citations (PDF) |
| 41 | Structure, Function, and Mechanism of the Nickel Metalloenzymes, CO Dehydrogenase, and Acetyl-CoA Synthase | 42.5 | 625 | Citations (PDF) |
| 42 | Protein/Protein Interactions in the Mammalian Heme Degradation Pathway | 1.3 | 34 | Citations (PDF) |
| 43 | Selective Visible-Light-Driven CO2 Reduction on a p-Type Dye-Sensitized NiO Photocathode | 11.7 | 107 | Citations (PDF) |
| 44 | Modulation of nuclear receptor function by cellular redox poise | 2.3 | 23 | Citations (PDF) |
| 45 | How Light-Harvesting Semiconductors Can Alter the Bias of Reversible Electrocatalysts in Favor of H2Production and CO2Reduction | 11.7 | 88 | Citations (PDF) |
| 46 | Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO2 Fixation | 42.5 | 2,170 | Citations (PDF) |
| 47 | A Unified Electrocatalytic Description of the Action of Inhibitors of Nickel Carbon Monoxide Dehydrogenase | 11.7 | 74 | Citations (PDF) |
| 48 | Investigations of Two Bidirectional Carbon Monoxide Dehydrogenases from Carboxydothermus hydrogenoformans by Protein Film Electrochemistry | 1.9 | 47 | Citations (PDF) |
| 49 | In vivo activation of methyl-coenzyme M reductase by carbon monoxide | 2.9 | 27 | Citations (PDF) |
| 50 | Visible light-driven CO2reduction by enzyme coupled CdS nanocrystals | 2.4 | 210 | Citations (PDF) |
| 51 | Transient B12-Dependent Methyltransferase Complexes Revealed by Small-Angle X-ray Scattering | 11.7 | 19 | Citations (PDF) |
| 52 | Radical reactions of thiamin pyrophosphate in 2-oxoacid oxidoreductases | 1.3 | 24 | Citations (PDF) |
| 53 | Visualizing molecular juggling within a B12-dependent methyltransferase complex | 30.7 | 92 | Citations (PDF) |
| 54 | Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from
Methanothermobacter marburgensis | 11.7 | 49 | Citations (PDF) |
| 55 | Evidence That Ferredoxin Interfaces with an Internal Redox Shuttle in Acetyl-CoA Synthase during Reductive Activation and Catalysis | 1.5 | 31 | Citations (PDF) |
| 56 | CO2 photoreduction at enzyme-modified metal oxide nanoparticles | 22.1 | 171 | Citations (PDF) |
| 57 | Metal centers in the anaerobic microbial metabolism of CO and CO2 | 1.7 | 72 | Citations (PDF) |
| 58 | Thiol-disulfide Redox Dependence of Heme Binding and Heme Ligand Switching in Nuclear Hormone Receptor Rev-erbβ | 1.3 | 93 | Citations (PDF) |
| 59 | Thiol/Disulfide Redox Switches in the Regulation of Heme Binding to Proteins | 4.1 | 47 | Citations (PDF) |
| 60 | Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2 | 1.7 | 15 | Citations (PDF) |
| 61 | Expanding the Biological Periodic Table | 4.7 | 3 | Citations (PDF) |
| 62 | Identification and Characterization of Oxalate Oxidoreductase, a Novel Thiamine Pyrophosphate-dependent 2-Oxoacid Oxidoreductase That Enables Anaerobic Growth on Oxalate | 1.3 | 28 | Citations (PDF) |
| 63 | Identification of a Thiol/Disulfide Redox Switch in the Human BK Channel That Controls Its Affinity for Heme and CO | 1.3 | 85 | Citations (PDF) |
| 64 | Infrared and EPR Spectroscopic Characterization of a Ni(I) Species Formed by Photolysis of a Catalytically Competent Ni(I)-CO Intermediate in the Acetyl-CoA Synthase Reaction | 1.5 | 48 | Citations (PDF) |
| 65 | Efficient and Clean Photoreduction of CO2 to CO by Enzyme-Modified TiO2 Nanoparticles Using Visible Light | 11.7 | 429 | Citations (PDF) |
| 66 | Structural Insight into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues, | 1.5 | 69 | Citations (PDF) |
| 67 | Observation of Organometallic and Radical Intermediates Formed during the Reaction of Methyl-Coenzyme M Reductase with Bromoethanesulfonate | 1.5 | 22 | Citations (PDF) |
| 68 | Detection of Organometallic and Radical Intermediates in the Catalytic Mechanism of Methyl-Coenzyme M Reductase Using the Natural Substrate Methyl-Coenzyme M and a Coenzyme B Substrate Analogue | 1.5 | 46 | Citations (PDF) |
| 69 | Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins | 1.6 | 12 | Citations (PDF) |
| 70 | Heme Regulatory Motifs in Heme Oxygenase-2 Form a Thiol/Disulfide Redox Switch That Responds to the Cellular Redox State | 1.3 | 72 | Citations (PDF) |
| 71 | Water−Gas Shift Reaction Catalyzed by Redox Enzymes on Conducting Graphite Platelets | 11.7 | 59 | Citations (PDF) |
| 72 | Geometric and Electronic Structures of the NiI and Methyl−NiIII Intermediates of Methyl-Coenzyme M Reductase | 1.5 | 52 | Citations (PDF) |
| 73 | Nickel-based Enzyme Systems | 1.3 | 373 | Citations (PDF) |
| 74 | Crystallographic Snapshots of Cyanide- and Water-Bound C-Clusters from Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase, | 1.5 | 81 | Citations (PDF) |
| 75 | Acetogenesis and the Wood–Ljungdahl pathway of CO2 fixation | 1.3 | 1,290 | Citations (PDF) |
| 76 | Enzymology of the Wood–Ljungdahl Pathway of Acetogenesis | 2.6 | 385 | Citations (PDF) |
| 77 | The complete genome sequence of
Moorella thermoacetica
(f.
Clostridium thermoaceticum
) | 2.6 | 281 | Citations (PDF) |
| 78 | Catalysis of Methyl Group Transfers Involving Tetrahydrofolate and B12 | 2.9 | 61 | Citations (PDF) |
| 79 | 13
C NMR Characterization of an Exchange Reaction between CO and CO
2
Catalyzed by Carbon Monoxide Dehydrogenase | 1.5 | 63 | Citations (PDF) |
| 80 | Characterization of the Thioether Product Formed from the Thiolytic Cleavage of the Alkyl−Nickel Bond in Methyl-Coenzyme M Reductase | 1.5 | 27 | Citations (PDF) |
| 81 | Dual Roles of an Essential Cysteine Residue in Activity of a Redox-regulated Bacterial Transcriptional Activator | 1.3 | 13 | Citations (PDF) |
| 82 | Pulse-Chase Studies of the Synthesis of Acetyl-CoA by Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase | 1.3 | 61 | Citations (PDF) |
| 83 | Xenon in and at the End of the Tunnel of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase, | 1.5 | 133 | Citations (PDF) |
| 84 | Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2 | 1.3 | 61 | Citations (PDF) |
| 85 | Evidence That the Heme Regulatory Motifs in Heme Oxygenase-2 Serve as a Thiol/Disulfide Redox Switch Regulating Heme Binding* | 1.3 | 81 | Citations (PDF) |
| 86 | Structural and Kinetic Evidence for an Extended Hydrogen-bonding Network in Catalysis of Methyl Group Transfer | 1.3 | 46 | Citations (PDF) |
| 87 | Characterization of Alkyl-Nickel Adducts Generated by Reaction of Methyl-Coenzyme M Reductase with Brominated Acids | 1.5 | 36 | Citations (PDF) |
| 88 | Biochemical and Spectroscopic Studies of the Electronic Structure and Reactivity of a Methyl−Ni Species Formed on Methyl-Coenzyme M Reductase | 11.7 | 65 | Citations (PDF) |
| 89 | Nickel and the carbon cycle | 2.3 | 161 | Citations (PDF) |
| 90 | Rapid and Efficient Electrocatalytic CO2/CO Interconversions by Carboxydothermus hydrogenoformans CO Dehydrogenase I on an Electrode | 11.7 | 214 | Citations (PDF) |
| 91 | Metals and Their Scaffolds To Promote Difficult Enzymatic Reactions | 42.5 | 199 | Citations (PDF) |
| 92 | Reduction and Oxidation of the Active Site Iron in Tyrosine Hydroxylase: Kinetics and Specificity | 1.5 | 50 | Citations (PDF) |
| 93 | Spectroscopic Studies of the Corrinoid/Iron−Sulfur Protein fromMoorella thermoacetica | 11.7 | 53 | Citations (PDF) |
| 94 | Spectroscopic and Computational Studies of Reduction of the Metal versus the Tetrapyrrole Ring of Coenzyme F430from Methyl-Coenzyme M Reductase† | 1.5 | 14 | Citations (PDF) |
| 95 | Pulsed Electron Paramagnetic Resonance Experiments Identify the Paramagnetic Intermediates in the Pyruvate Ferredoxin Oxidoreductase Catalytic Cycle | 11.7 | 38 | Citations (PDF) |
| 96 | EPR Spectroscopic and Computational Characterization of the Hydroxyethylidene-Thiamine Pyrophosphate Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase† | 1.5 | 74 | Citations (PDF) |
| 97 | CprK Crystal Structures Reveal Mechanism for Transcriptional Control of Halorespiration | 1.3 | 34 | Citations (PDF) |
| 98 | Spectroscopic and Kinetic Studies of the Reaction of Bromopropanesulfonate with Methyl-coenzyme M Reductase | 1.3 | 30 | Citations (PDF) |
| 99 | Transcriptional Activation of Dehalorespiration | 1.3 | 28 | Citations (PDF) |
| 100 | EPR and Infrared Spectroscopic Evidence That a Kinetically Competent Paramagnetic Intermediate is Formed When Acetyl-Coenzyme A Synthase Reacts with CO | 11.7 | 65 | Citations (PDF) |
| 101 | Mechanism of 4-(β-D-Ribofuranosyl)aminobenzene 5′-Phosphate Synthase, a Key Enzyme in the Methanopterin Biosynthetic Pathway | 1.3 | 23 | Citations (PDF) |
| 102 | Regulation of Anaerobic Dehalorespiration by the Transcriptional Activator CprK | 1.3 | 42 | Citations (PDF) |
| 103 | Life with Carbon Monoxide | 3.9 | 399 | Citations (PDF) |
| 104 | CO-Induced Structural Rearrangement of the C Cluster inCarboxydothermus hydrogenoformansCO DehydrogenaseEvidence from Ni K-Edge X-ray Absorption Spectroscopy† | 1.5 | 36 | Citations (PDF) |
| 105 | Evidence That NiNi Acetyl-CoA Synthase Is Active and That the CuNi Enzyme Is Not† | 1.5 | 86 | Citations (PDF) |
| 106 | Nickel Oxidation States of F430Cofactor in Methyl-Coenzyme M Reductase | 11.7 | 56 | Citations (PDF) |
| 107 | Pyruvate Ferredoxin Oxidoreductase and Its Radical Intermediate | 42.5 | 255 | Citations (PDF) |
| 108 | Rapid Ligand Exchange in the MCRred1 Form of Methyl-coenzyme M Reductase | 11.7 | 18 | Citations (PDF) |
| 109 | The Many Faces of Vitamin B12: Catalysis by Cobalamin-Dependent Enzymes | 14.0 | 783 | Citations (PDF) |
| 110 | Infrared Studies of Carbon Monoxide Binding to Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase from Moorella thermoacetica | 1.5 | 62 | Citations (PDF) |
| 111 | Functional copper at the acetyl-CoA synthase active site | 5.2 | 71 | Citations (PDF) |
| 112 | Targeting Methanopterin Biosynthesis ToInhibitMethanogenesis | 2.4 | 35 | Citations (PDF) |
| 113 | Spectroscopic and computational characterization of the nickel-containing F430 cofactor of methyl-coenzyme M reductase | 1.7 | 27 | Citations (PDF) |
| 114 | Rapid Kinetic Studies of Acetyl-CoA Synthesis: Evidence Supporting the Catalytic Intermediacy of a Paramagnetic NiFeC Species in the Autotrophic Wood−Ljungdahl Pathway† | 1.5 | 95 | Citations (PDF) |
| 115 | A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/ Acetyl-CoA Synthase | 26.1 | 552 | Citations (PDF) |
| 116 | The Roles of Coenzyme A in the Pyruvate:Ferredoxin Oxidoreductase Reaction Mechanism: Rate Enhancement of Electron Transfer from a Radical Intermediate to an Iron−Sulfur Cluster† | 1.5 | 57 | Citations (PDF) |
| 117 | X-ray Absorption and Resonance Raman Studies of Methyl-Coenzyme M Reductase Indicating That Ligand Exchange and Macrocycle Reduction Accompany Reductive Activation† | 11.7 | 48 | Citations (PDF) |
| 118 | Acetyl Coenzyme A Synthesis from Unnatural Methylated Corrinoids: Requirement for “Base-Off” Coordination at Cobalt | 11.7 | 33 | Citations (PDF) |
| 119 | Cryoreduction of Methyl-Coenzyme M Reductase: EPR Characterization of Forms, MCRox1and MCRred1 | 11.7 | 62 | Citations (PDF) |
| 120 | Mechanistic Studies of Methane Biogenesis by Methyl-Coenzyme M Reductase: Evidence that Coenzyme B Participates in Cleaving the C−S Bond of Methyl-Coenzyme M† | 1.5 | 67 | Citations (PDF) |
| 121 | Redox Centers of 4-Hydroxybenzoyl-CoA Reductase, a Member of the Xanthine Oxidase Family of Molybdenum-containing Enzymes | 1.3 | 45 | Citations (PDF) |
| 122 | Characterization of the Intramolecular Electron Transfer Pathway from 2-Hydroxyphenazine to the Heterodisulfide Reductase fromMethanosarcina thermophila | 1.3 | 33 | Citations (PDF) |
| 123 | Characterization of the B12- and Iron-Sulfur-containing Reductive Dehalogenase fromDesulfitobacterium chlororespirans | 1.3 | 81 | Citations (PDF) |
| 124 | Characterization of a Three-Component Vanillate
O
-Demethylase from
Moorella thermoacetica | 2.2 | 103 | Citations (PDF) |
| 125 | Evidence for Intersubunit Communication during Acetyl-CoA Cleavage by the Multienzyme CO Dehydrogenase/Acetyl-CoA Synthase Complex from Methanosarcina thermophila | 1.3 | 26 | Citations (PDF) |
| 126 | Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase | 2.4 | 81 | Citations (PDF) |
| 127 | The Role of Pyruvate Ferredoxin Oxidoreductase in Pyruvate Synthesis during Autotrophic Growth by the Wood-Ljungdahl Pathway | 1.3 | 199 | Citations (PDF) |
| 128 | Channeling of Carbon Monoxide during Anaerobic Carbon Dioxide Fixation† | 1.5 | 95 | Citations (PDF) |
| 129 | On the Assignment of Nickel Oxidation States of the Ox1, Ox2 Forms of Methyl−Coenzyme M Reductase | 11.7 | 65 | Citations (PDF) |
| 130 | Characterization of Heterogeneous Nickel Sites in CO Dehydrogenases fromClostridium thermoaceticumandRhodospirillum rubrumby Nickel L-Edge X-ray Spectroscopy | 11.7 | 66 | Citations (PDF) |
| 131 | The Role of an Iron-Sulfur Cluster in an Enzymatic Methylation Reaction | 1.3 | 70 | Citations (PDF) |
| 132 | ENDOR Studies of Pyruvate:Ferredoxin Oxidoreductase Reaction Intermediates | 11.7 | 10 | Citations (PDF) |
| 133 | Binding of (6R,S)-Methyltetrahydrofolate to Methyltransferase fromClostridium thermoaceticum: Role of Protonation of Methyltetrahydrofolate in the Mechanism of Methyl Transfer† | 1.5 | 22 | Citations (PDF) |
| 134 | Mechanism of Transfer of the Methyl Group from (6S)-Methyltetrahydrofolate to the Corrinoid/Iron−Sulfur Protein Catalyzed by the Methyltransferase fromClostridium thermoaceticum: A Key Step in the Wood−Ljungdahl Pathway of Acetyl-CoA Synthesis† | 1.5 | 37 | Citations (PDF) |
| 135 | Nitrate-Dependent Regulation of Acetate Biosynthesis and Nitrate Respiration by
Clostridium thermoaceticum | 2.2 | 34 | Citations (PDF) |
| 136 | Nickel biochemistry | 4.6 | 118 | Citations (PDF) |
| 137 | The F420H2:heterodisulfide oxidoreductase system fromMethanosarcinaspecies | 1.8 | 44 | Citations (PDF) |
| 138 | Activation of Methyl-SCoM Reductase to High Specific Activity after Treatment of Whole Cells with Sodium Sulfide† | 1.5 | 68 | Citations (PDF) |
| 139 | Role of the [4Fe-4S] Cluster in Reductive Activation of the Cobalt Center of the Corrinoid Iron−Sulfur Protein from Clostridium thermoaceticum during Acetate Biosynthesis | 1.5 | 71 | Citations (PDF) |
| 140 | Purification and Properties of the Heme- and Iron−Sulfur-Containing Heterodisulfide Reductase from Methanosarcina thermophila | 1.5 | 64 | Citations (PDF) |
| 141 | Electrochemical and Spectroscopic Properties of the Iron-Sulfur Flavoprotein from Methanosarcina thermophila | 1.3 | 18 | Citations (PDF) |
| 142 | Nucleotide Excision Repair in the Third Kingdom | 2.2 | 47 | Citations (PDF) |
| 143 | Mechanism of Carbon Monoxide Oxidation by the Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase from Clostridium thermoaceticum: Kinetic Characterization of the Intermediates | 1.5 | 65 | Citations (PDF) |
| 144 | Mechanism of the Clostridium thermoaceticum Pyruvate:Ferredoxin Oxidoreductase: Evidence for the Common Catalytic Intermediacy of the Hydroxyethylthiamine Pyropyrosphate Radical | 1.5 | 77 | Citations (PDF) |
| 145 | The Eastern and Western branches of the Wood/Ljungdahl pathway: how the East and West were won | 3.1 | 94 | Citations (PDF) |
| 146 | Nickel-Containing Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase , | 42.5 | 355 | Citations (PDF) |
| 147 | A Conformational Change in the Methyltransferase fromClostridium thermoaceticumFacilitates the Methyl Transfer from (6S)-Methyltetrahydrofolate to the Corrinoid/Iron−Sulfur Protein in the Acetyl-CoA Pathway† | 1.5 | 17 | Citations (PDF) |
| 148 | Raman and Infrared Spectroscopy of Cyanide-Inhibited CO Dehydrogenase/Acetyl-CoA Synthase fromClostridium thermoaceticum: Evidence for Bimetallic Enzymatic CO Oxidation | 11.7 | 24 | Citations (PDF) |
| 149 | Evidence That Carbon Monoxide Is an Obligatory Intermediate in Anaerobic Acetyl-CoA Synthesis† | 1.5 | 59 | Citations (PDF) |
| 150 | Unleashing Hydrogenase Activity in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase and Pyruvate:Ferredoxin Oxidoreductase† | 1.5 | 81 | Citations (PDF) |
| 151 | The role of nickel in acetyl-CoA synthesis by the bifunctional enzyme CO dehydrogenase/acetyl-CoA synthase: enzymology and model chemistry | 1.7 | 20 | Citations (PDF) |
| 152 | Preliminary X-ray crystallographic study of methyltetrahydrofolate: corrinoid/iron sulfur protein methyltransferase fromClostridium thermoaceticum | 3.1 | 3 | Citations (PDF) |
| 153 | Mechanistic Studies of the Methyltransferase from Clostridium thermoaceticum: Origin of the pH Dependence of the Methyl Group Transfer from Methyl Tetrahydrofolate to the Corrinoid/Iron-Sulfur Protein | 1.5 | 50 | Citations (PDF) |
| 154 | Mechanism of CO oxidation by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by anions | 1.5 | 65 | Citations (PDF) |
| 155 | Azide Binding to Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum | 11.7 | 16 | Citations (PDF) |
| 156 | n-Butyl isocyanide: A structural and functional analog of carbon monoxide for carbon monoxide dehydrogenase from Clostridium thermoaceticum | 11.7 | 19 | Citations (PDF) |
| 157 | Freeze-quench resonance Raman spectroscopic evidence for an Fe-CO adduct during acetyl-CoA synthesis and Ni involvement in CO oxidation by carbon monoxide dehydrogenase from Clostridium thermoaceticum | 11.7 | 30 | Citations (PDF) |
| 158 | Structural and Electronic Factors in Heterolytic Cleavage: Formation of the Co(I) Intermediate in the Corrinoid/Iron-Sulfur Protein from Clostridium thermoaceticum | 1.5 | 26 | Citations (PDF) |
| 159 | Hydroxybenzoyl-CoA reductase: coupling kinetics and electrochemistry to derive enzyme mechanisms | 1.5 | 18 | Citations (PDF) |
| 160 | Characterization of the iron-sulfur clusters in ferredoxin from acetate-grown Methanosarcina thermophila | 2.2 | 18 | Citations (PDF) |
| 161 | The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum | 2.2 | 64 | Citations (PDF) |
| 162 | Binding of Carbon Disulfide to the Site of Acetyl-CoA Synthesis by the Nickel-Iron-Sulfur Protein, Carbon Monoxide Dehydrogenase, from Clostridium thermoaceticum | 1.5 | 52 | Citations (PDF) |
| 163 | Anaerobic Pathway for Conversion of the Methyl Group of Aromatic Methyl Ethers to Acetic Acid by Clostridium thermoaceticum | 1.5 | 50 | Citations (PDF) |
| 164 | Characterization of the carbonylation and methylation sites in carbon monoxide dehydrogenase from clostridium thermoaceticum. | 2.3 | 1 | Citations (PDF) |
| 165 | Kinetic evidence that carbon monoxide dehydrogenase catalyzes the oxidation of carbon monoxide and the synthesis of acetyl-CoA at separate metal clusters | 11.7 | 78 | Citations (PDF) |
| 166 | X-ray absorption spectroscopy of the corrinoid/iron-sulfur protein involved in acetyl coenzyme A synthesis by Clostridium thermoaceticum | 11.7 | 35 | Citations (PDF) |
| 167 | Characterization of the carbon monoxide binding site of carbon monoxide dehydrogenase from Clostridium thermoaceticum by infrared spectroscopy | 11.7 | 75 | Citations (PDF) |
| 168 | Acetyl-coenzyme A synthesis from methyltetrahydrofolate, CO, and coenzyme A by enzymes purified from Clostridium thermoaceticum: attainment of in vivo rates and identification of rate-limiting steps | 2.2 | 44 | Citations (PDF) |
| 169 | Enzymology of the Acetyl-CoA Pathway of CO2Fixation | 3.9 | 264 | Citations (PDF) |
| 170 | Characterization of the nickel-iron-carbon complex formed by reaction of carbon monoxide with the carbon monoxide dehydrogenase from Clostridium thermoaceticum by Q-band ENDOR | 1.5 | 104 | Citations (PDF) |
| 171 | Reductive activation of the coenzyme A/acetyl-CoA isotopic exchange reaction catalyzed by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by nitrous oxide and carbon monoxide | 1.3 | 66 | Citations (PDF) |
| 172 | The acetyl-CoA synthase fromClostridium thermoaceticum: from gene cluster to achive-site metal clusters | 1.1 | 11 | Citations (PDF) |
| 173 | Mechanism of reductive activation of cobalamin-dependent methionine synthase: an electron paramagnetic resonance spectroelectrochemical study | 1.5 | 161 | Citations (PDF) |
| 174 | CO dehydrogenase from Clostridium thermoaceticum. EPR and electrochemical studies in CO2 and argon atmospheres. | 1.3 | 131 | Citations (PDF) |
| 175 | Mössbauer study of CO dehydrogenase from Clostridium thermoaceticum. | 1.3 | 105 | Citations (PDF) |
| 176 | Controlled potential enzymology of methyl transfer reactions involved in acetyl-CoA synthesis by CO dehydrogenase and the corrinoid/iron-sulfur protein from Clostridium thermoaceticum. | 1.3 | 82 | Citations (PDF) |
| 177 | The acetyl-CoA synthase from Clostridium thermoaceticum: from gene cluster to achive-site metal clusters | 1.1 | 0 | Citations (PDF) |
| 178 | A spectroelectrochemical cell designed for low temperature electron paramagnetic resonance titration of oxygen-sensitive proteins | 2.0 | 36 | Citations (PDF) |
| 179 | Spectroelectrochemical studies of the corrinoid/iron-sulfur protein involved in acetyl coenzyme A synthesis by Clostridium thermoaceticum | 1.5 | 100 | Citations (PDF) |
| 180 | Cloning and expression of the gene cluster encoding key proteins involved in acetyl-CoA synthesis in Clostridium thermoaceticum: CO dehydrogenase, the corrinoid/Fe-S protein, and methyltransferase. | 5.2 | 67 | Citations (PDF) |
| 181 | Mössbauer, EPR, and optical studies of the corrinoid/iron-sulfur protein involved in the synthesis of acetyl coenzyme A by Clostridium thermoaceticum. | 1.3 | 153 | Citations (PDF) |
| 182 | Evidence that an iron-nickel-carbon complex is formed by reaction of CO with the CO dehydrogenase from Clostridium thermoaceticum. | 5.2 | 177 | Citations (PDF) |
| 183 | Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis. | 1.3 | 238 | Citations (PDF) |
| 184 | Hydrogenase from Acetobacterium woodii | 2.1 | 59 | Citations (PDF) |
| 185 | Purification and properties of NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Acetobacterium woodii. | 1.3 | 61 | Citations (PDF) |
| 186 | Characterization of ferredoxin, flavodoxin, and rubredoxin from Clostridium formicoaceticum grown in media with high and low iron contents | 2.2 | 53 | Citations (PDF) |
| 187 | 13C and 61Ni isotope substitutions confirm the presence of a nickel(III)-carbon species in acetogenic CO dehydrogenases | 1.5 | 103 | Citations (PDF) |
| 188 | Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein. | 1.3 | 228 | Citations (PDF) |
| 189 | Isolation of carbon monoxide dehydrogenase from Acetobacterium woodii and comparison of its properties with those of the Clostridium thermoaceticum enzyme | 2.2 | 148 | Citations (PDF) |
| 190 | EPR evidence for nickel-substrate interaction in carbon monoxide dehydrogenase from Clostridium thermoaceticum | 1.5 | 104 | Citations (PDF) |
| 191 | Levels of enzymes involved in the synthesis of acetate from CO2 in Clostridium thermoautotrophicum | 2.2 | 56 | Citations (PDF) |
| 192 | Heme and CO metabolism by the canonical human heme oxygenases | 2.3 | 0 | Citations (PDF) |
| 193 | Investigating weak axial ligation in corrinoids by X-ray absorption spectroscopy: Implications for corrinoid iron-sulfur protein | 2.3 | 1 | Citations (PDF) |
