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Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
inferred← citeshttps://doi.org/10.1016/j.bbabio.2012.04.012openalex-snapshot
Evolution and diversification of Group 1 [NiFe] hydrogenases. Is there a phylogenetic marker for O2-tolerance?
inferred← citeshttps://doi.org/10.1016/j.bbabio.2012.06.337openalex-snapshot
Membrane-bound respiratory nitrate reductase functioning: It takes two to tango
inferred← citeshttps://doi.org/10.1016/j.bbabio.2012.06.385openalex-snapshot
The Paramagnetic and Redox Properties of the Hemes of E. coli Nitrate Reductase
inferred← citeshttps://doi.org/10.1016/j.bbabio.2012.09.001openalex-snapshot
Unifying concepts in anaerobic respiration: Insights from dissimilatory sulfur metabolism
inferred← citeshttps://doi.org/10.1016/j.bbabio.2012.09.005openalex-snapshot
On the universal core of bioenergetics
inferred← citeshttps://doi.org/10.1016/j.bbabio.2012.10.002openalex-snapshot
Denitrification and aerobic respiration, hybrid electron transport chains and co-evolution
inferred← citeshttps://doi.org/10.1016/j.bbabio.2013.01.011openalex-snapshot
The prokaryotic Mo/W-bisPGD enzymes family: A catalytic workhorse in bioenergetic
inferred← citeshttps://doi.org/10.1016/j.bbabio.2013.02.009openalex-snapshot
A variant conferring cofactor-dependent assembly of Escherichia coli dimethylsulfoxide reductase
inferred← citeshttps://doi.org/10.1016/j.bbabio.2013.02.012openalex-snapshot
The di-heme family of respiratory complex II enzymes
inferred← citeshttps://doi.org/10.1016/j.bbabio.2013.10.013openalex-snapshot
Reductive activation in periplasmic nitrate reductase involves chemical modifications of the Mo-cofactor beyond the first coordination sphere of the metal ion
inferred← citeshttps://doi.org/10.1016/j.bbabio.2015.05.001openalex-snapshot
Demethylmenaquinol is a substrate of Escherichia coli nitrate reductase A (NarGHI) and forms a stable semiquinone intermediate at the NarGHI quinol oxidation site
inferred← citeshttps://doi.org/10.1016/j.bbabio.2015.06.007openalex-snapshot
Reductive activation of E. coli respiratory nitrate reductase
inferred← citeshttps://doi.org/10.1016/j.bbabio.2015.11.001openalex-snapshot
Supramolecular organization of bacterial aerobic respiratory chains: From cells and back
inferred← citeshttps://doi.org/10.1016/j.bbabio.2016.03.028openalex-snapshot
Exploring membrane respiratory chains
inferred← citeshttps://doi.org/10.1016/j.bbabio.2019.01.003openalex-snapshot
Tuning the redox properties of a [4Fe-4S] center to modulate the activity of Mo-bisPGD periplasmic nitrate reductase
inferred← citeshttps://doi.org/10.1016/j.bbabio.2020.148203openalex-snapshot
1,2H hyperfine spectroscopy and DFT modeling unveil the demethylmenasemiquinone binding mode to E. coli nitrate reductase A (NarGHI)
inferred← citeshttps://doi.org/10.1016/j.bbabio.2020.148279openalex-snapshot
Sulfite oxidation by the quinone-reducing molybdenum sulfite dehydrogenase SoeABC from the bacterium Aquifex aeolicus
inferred← citeshttps://doi.org/10.1016/j.bbabio.2021.148401openalex-snapshot
The dyad of the Y-junction- and a flavin module unites diverse redox enzymes
inferred← citeshttps://doi.org/10.1016/j.bbabio.2021.148492openalex-snapshot
The HydS C-terminal domain of the Thiocapsa bogorovii HydSL hydrogenase is involved in membrane anchoring and electron transfer
inferred← citeshttps://doi.org/10.1016/j.bbagen.2005.02.008openalex-snapshot
Isolation and spectroscopic characterization of the membrane-bound nitrate reductase from Pseudomonas chlororaphis DSM 50135
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2010.01.019openalex-snapshot
Biogenesis of membrane bound respiratory complexes in Escherichia coli
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.02.007openalex-snapshot
Cell biology of molybdenum in plants and humans
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2014.09.021openalex-snapshot
The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria
inferred← citeshttps://doi.org/10.1016/j.bbamem.2003.10.016openalex-snapshot
Glutamate 87 is important for menaquinol binding in DmsC of the DMSO reductase (DmsABC) from Escherichia coli
inferred← citeshttps://doi.org/10.1016/j.bbamem.2004.05.012openalex-snapshot
How lipids affect the activities of integral membrane proteins
inferred← citeshttps://doi.org/10.1016/j.bbamem.2007.07.020openalex-snapshot
Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis
inferred← citeshttps://doi.org/10.1016/j.bbamem.2007.09.002openalex-snapshot
The prokaryotic complex iron–sulfur molybdoenzyme family
inferred← citeshttps://doi.org/10.1016/j.bbamem.2014.08.020openalex-snapshot
‘Come into the fold’: A comparative analysis of bacterial redox enzyme maturation protein members of the NarJ subfamily
inferred← citeshttps://doi.org/10.1016/j.bbamem.2014.08.021openalex-snapshot
Cardiolipin interaction with subunit c of ATP synthase: Solid-state NMR characterization
inferred← citeshttps://doi.org/10.1016/j.bbrc.2004.06.086openalex-snapshot
Mutagenesis study on amino acids around the molybdenum centre of the periplasmic nitrate reductase from Ralstonia eutropha
inferred← citeshttps://doi.org/10.1016/j.biochi.2010.06.003openalex-snapshot
Thermostable properties of the periplasmic selenate reductase from Thauera selenatis
inferred← citeshttps://doi.org/10.1016/j.biortech.2024.131986openalex-snapshot
Long-term stability of comammox Nitrospira under weakly acidic conditions and their acid-adaptive mechanisms revealed by genome-centric metatranscriptomics
inferred← citeshttps://doi.org/10.1016/j.biortech.2025.133388openalex-snapshot
Deciphering effect of complex organics on Anammox-sulfide autotrophic denitrification coupling system for landfill leachate treatment
inferred← citeshttps://doi.org/10.1016/j.cbpa.2007.02.027openalex-snapshot
Adding handles to unhandy substrates: anaerobic hydrocarbon activation mechanisms
inferred← citeshttps://doi.org/10.1016/j.cbpa.2013.12.015openalex-snapshot
Alternative FeS cluster ligands: tuning redox potentials and chemistry
inferred← citeshttps://doi.org/10.1016/j.ccr.2010.01.017openalex-snapshot
Dithiolene complexes and the nature of molybdopterin
inferred← citeshttps://doi.org/10.1016/j.ccr.2010.10.017openalex-snapshot
Comparative molecular chemistry of molybdenum and tungsten and its relation to hydroxylase and oxotransferase enzymes
inferred← citeshttps://doi.org/10.1016/j.ccr.2010.11.017openalex-snapshot
Structural aspects of mononuclear Mo/W-enzymes
inferred← citeshttps://doi.org/10.1016/j.ccr.2010.11.027openalex-snapshot
Bioinorganic chemistry of molybdenum and tungsten enzymes: A structural–functional modeling approach
inferred← citeshttps://doi.org/10.1016/j.ccr.2010.12.031openalex-snapshot
Molybdenum enzymes in bacteria and their maturation
inferred← citeshttps://doi.org/10.1016/j.ccr.2011.01.054openalex-snapshot
Molybdenum cofactor biosynthesis in plants and humans
inferred← citeshttps://doi.org/10.1016/j.ccr.2011.01.056openalex-snapshot
Spectroscopic studies of molybdenum and tungsten enzymes
inferred← citeshttps://doi.org/10.1016/j.ccr.2011.02.010openalex-snapshot
Pterin chemistry and its relationship to the molybdenum cofactor
inferred← citeshttps://doi.org/10.1016/j.ccr.2012.05.020openalex-snapshot
Periplasmic nitrate reductases and formate dehydrogenases: Biological control of the chemical properties of Mo and W for fine tuning of reactivity, substrate specificity and metabolic role
inferred← citeshttps://doi.org/10.1016/j.ccr.2019.05.005openalex-snapshot
Molybdenum and tungsten enzymes redox properties – A brief overview
inferred← citeshttps://doi.org/10.1016/j.ccr.2020.213476openalex-snapshot
Nitrate-nitrite fate and oxygen sensing in dormant Mycobacterium tuberculosis: A bioinorganic approach highlighting the importance of transition metals
inferred← citeshttps://doi.org/10.1016/j.cej.2024.149592openalex-snapshot
Unraveling metabolic fate of a veterinary antibiotic thiamphenicol via the multi-omic approach
inferred← citeshttps://doi.org/10.1016/j.cej.2024.154410openalex-snapshot
Multi-omics analysis for mechanistic understanding of microbial-mediated synthesis of silver nanoparticles
inferred← citeshttps://doi.org/10.1016/j.cej.2025.165884openalex-snapshot
Reversing N-intermediate adsorption configuration over Mo Fe diatomic sites enables enhanced nitrate reduction
inferred← citeshttps://doi.org/10.1016/j.chemosphere.2021.131315openalex-snapshot
Catalytic enhancement of hydrogenation reduction and oxygen transfer reaction for perchlorate removal: A review
inferred← citeshttps://doi.org/10.1016/j.chemphyslip.2006.02.005openalex-snapshot
Lipid conformation in crystalline bilayers and in crystals of transmembrane proteins
inferred← citeshttps://doi.org/10.1016/j.chempr.2023.05.037openalex-snapshot
Advances in ammonia electrosynthesis from ambient nitrate/nitrite reduction
inferred← citeshttps://doi.org/10.1016/j.compbiolchem.2019.01.014openalex-snapshot
Identification of coenzyme-binding proteins with machine learning algorithms
inferred← citeshttps://doi.org/10.1016/j.csbj.2019.05.005openalex-snapshot
Interfaces Between Alpha-helical Integral Membrane Proteins: Characterization, Prediction, and Docking
inferred← citeshttps://doi.org/10.1016/j.ecoenv.2018.09.104openalex-snapshot
Effect of Fe(II) on reactivity of heterotrophic denitrifiers in the remediation of nitrate- and Fe(II)-contaminated groundwater
inferred← citeshttps://doi.org/10.1016/j.envres.2026.124428openalex-snapshot
Agriculture alters protein evolution of respiratory nitrate reductase in soil bacteria at a global scale
inferred← citeshttps://doi.org/10.1016/j.febslet.2009.12.060openalex-snapshot
Determinants of specificity at the protein–lipid interface in membranes
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2025.08.046openalex-snapshot
Coproheme decarboxylase from Bacillus subtilis is required for bacterial growth and heme b biosynthesis under anaerobic conditions
inferred← citeshttps://doi.org/10.1016/j.gca.2022.04.019openalex-snapshot
Copper availability governs nitrous oxide accumulation in wetland soils and stream sediments
inferred← citeshttps://doi.org/10.1016/j.ibiod.2008.01.009openalex-snapshot
Anaerobic domestic wastewater treatment with bamboo carrier anaerobic baffled reactor
inferred← citeshttps://doi.org/10.1016/j.ica.2006.10.041openalex-snapshot
Design, synthesis, and characterization of a sterically encumbered dioxo molybdenum (VI) core
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2024.129620openalex-snapshot
Complementary hydrophobic interaction of the redox enzyme maturation protein NarJ with the signal peptide of the respiratory nitrate reductase NarG
inferred← citeshttps://doi.org/10.1016/j.ijfoodmicro.2021.109201openalex-snapshot
Survival and transcriptomic response of Salmonella enterica on fresh-cut fruits
inferred← citeshttps://doi.org/10.1016/j.jbiotec.2023.11.007openalex-snapshot
Catalytic and anti-cancer properties of platinum, gold, silver, and bimetallic Au-Ag nanoparticles synthesized by Bacillus sp. bacteria
inferred← citeshttps://doi.org/10.1016/j.jece.2026.122362openalex-snapshot
Denitrification powered by diverse electron donors: A mechanistic synthesis
inferred← citeshttps://doi.org/10.1016/j.jelechem.2013.01.030openalex-snapshot
Induced peroxidase activity of haem containing nitrate reductases revealed by protein film electrochemistry
inferred← citeshttps://doi.org/10.1016/j.jes.2026.105817openalex-snapshot
Natural iron minerals modulate denitrification pathways in bioelectrochemical systems: An evidence chain established using electrochemistry, extracellular polymeric substances and metagenomics
inferred← citeshttps://doi.org/10.1016/j.jhazmat.2024.133877openalex-snapshot
Control of tobacco-specific nitrosamines by the Bacillus siamensis: Strain isolation, genome sequencing, mechanism analysis and genetic engineering
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2004.09.024openalex-snapshot
Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme?copper oxidase type
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2005.11.024openalex-snapshot
Bacterial nitrate reductases: Molecular and biological aspects of nitrate reduction
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2006.09.003openalex-snapshot
Metalloenzymes of the denitrification pathway
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2007.07.012openalex-snapshot
Synthesis, characterization, and spectroscopy of model molybdopterin complexes
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2014.05.006openalex-snapshot
Mechanistic basis for the enantioselectivity of the anaerobic hydroxylation of alkylaromatic compounds by ethylbenzene dehydrogenase
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2017.04.027openalex-snapshot
Reaction mechanism of sterol hydroxylation by steroid C25 dehydrogenase – Homology model, reactivity and isoenzymatic diversity
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2021.111687openalex-snapshot
Sulfide and transition metals - A partnership for life
inferred← citeshttps://doi.org/10.1016/j.jiph.2020.08.004openalex-snapshot
In silico prediction of silver nitrate nanoparticles and Nitrate Reductase A (NAR A) interaction in the treatment of infectious disease causing clinical strains of E. coli
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.05.066openalex-snapshot
Quinol Oxidation by c-Type Cytochromes: Structural Characterization of the Menaquinol Binding Site of NrfHA
inferred← citeshttps://doi.org/10.1016/j.jsb.2018.01.010openalex-snapshot
Structure and electrochemistry of proteins harboring iron-sulfur clusters of different nuclearities. Part II. [4Fe-4S] and [3Fe-4S] iron-sulfur proteins
inferred← citeshttps://doi.org/10.1016/j.molstruc.2020.129867openalex-snapshot
Aiding a Better Understanding of Molybdopterin: Syntheses, Structures, and pKa Value Determinations of Varied Pterin-Derived Organic Scaffolds Including Oxygen, Sulfur and Phosphorus Bearing Substituents
inferred← citeshttps://doi.org/10.1016/j.pep.2017.03.019openalex-snapshot
Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization
inferred← citeshttps://doi.org/10.1016/j.pep.2026.106906openalex-snapshot
Expression, purification and biochemical characterization of the periplasmic nitrate reductase NapA from Magnetospirillum gryphiswaldense MSR-1
inferred← citeshttps://doi.org/10.1016/j.plaphy.2011.07.007openalex-snapshot
Enzyme kinetics, inhibitors, mutagenesis and electron paramagnetic resonance analysis of dual-affinity nitrate reductase in unicellular N2-fixing cyanobacterium Cyanothece sp. PCC 8801
inferred← citeshttps://doi.org/10.1016/j.poly.2009.10.018openalex-snapshot
The difference one ligand atom makes – An altered oxygen transfer reaction mechanism caused by an exchange of selenium for sulfur
inferred← citeshttps://doi.org/10.1016/j.scitotenv.2020.139080openalex-snapshot
A critical review of aerobic denitrification: Insights into the intracellular electron transfer
inferred← citeshttps://doi.org/10.1016/j.str.2003.11.020openalex-snapshot
Architecture of NarGH Reveals a Structural Classification of Mo-bisMGD Enzymes
inferred← citeshttps://doi.org/10.1016/j.str.2006.07.001openalex-snapshot
Crystal Structure of Ethylbenzene Dehydrogenase from Aromatoleum aromaticum
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