Results 11 to 20 of about 8,200 (237)
The active site structure and catalytic mechanism of arsenite oxidase [PDF]
Scientific Reports, 2017 Arsenite oxidase is thought to be an ancient enzyme, originating before the divergence of the Archaea and the Bacteria. We have investigated the nature of the molybdenum active site of the arsenite oxidase from the Alphaproteobacterium Rhizobium sp. str.
Thomas P. Warelow +4 more
doaj +2 more sources
Classifying the metal dependence of uncharacterized nitrogenases [PDF]
Frontiers in Microbiology, 2013 Nitrogenase enzymes have evolved complex iron-sulfur (Fe-S) containing cofactors that most commonly contain molybdenum (MoFe, Nif) as a heterometal but also exist as vanadium (VFe, Vnf) and heterometal independent (Fe-only, Anf) forms.
Shawn E Mcglynn +3 more
doaj +4 more sources
Adaptations of Escherichia coli strains to oxidative stress are reflected in properties of their structural proteomes. [PDF]
, 2020 BACKGROUND:The reconstruction of metabolic networks and the three-dimensional coverage of protein structures have reached the genome-scale in the widely studied Escherichia coli K-12 MG1655 strain.
Catoiu, Edward +6 more
core +2 more sources
Current knowledge and recent advances in understanding metabolism of the model cyanobacterium Synechocystis sp. PCC 6803 [PDF]
, 2020 Cyanobacteria are key organisms in the global ecosystem, useful models for studying metabolic and physiological processes conserved in photosynthetic organisms, and potential renewable platforms for production of chemicals.
Lea-Smith, David +2 more
core +3 more sources
mBio, 2022 Engineering plants to synthesize nitrogenase and assimilate atmospheric N2 will reduce crop dependency on industrial N fertilizers. This technology can be achieved by expressing prokaryotic nitrogen fixation gene products for the assembly of a functional
Xi Jiang +8 more
doaj +1 more source
Identification of YdhV as the first molybdoenzyme binding a Bis-Mo-MPT cofactor in escherichia coli [PDF]
, 2019 The oxidoreductase YdhV in Escherichia coli has been predicted to belong to the family of molybdenum/tungsten cofactor (Moco/Wco)-containing enzymes. In this study, we characterized the YdhV protein in detail, which shares amino acid sequence homology ...
Dau, Holger +7 more
core +1 more source
Journal of Biological Chemistry, 2013 The transition element molybdenum needs to be complexed by a special cofactor to gain catalytic activity. Molybdenum is bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants, is the active compound at the catalytic site of all molybdenum-containing enzymes in nature, except bacterial molybdenum nitrogenase.
openaire +2 more sources
Functional studies on oligotropha carboxidovorans molybdenum–copper CO dehydrogenase produced in escherichia coli [PDF]
, 2018 The Mo/Cu-dependent CO dehydrogenase (CODH) from Oligotropha carboxidovorans is an enzyme that is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons. Despite the close to atomic resolution structure (1.1 Å),
Duffus, Benjamin R. +3 more
core +1 more source
Anomalous supply of bioessential molybdenum in mid-Proterozoic surface environments [PDF]
, 2016 We are grateful to A. Sandison and W. Thayalon for skilled technical support, and Mike Porter and an anonymous reviewer, who helped to clarify the manuscript.Peer ...
Lindgren, Paula, Parnell, John
core +1 more source
Molybdenum cofactor deficiency: A natural history [PDF]
Journal of Inherited Metabolic Disease, 2022 AbstractMolybdenum cofactor deficiency (MoCD) includes three ultrarare autosomal recessive inborn errors of metabolism (MoCD type A [MoCD‐A], MoCD‐B, and MoCD‐C) that cause sulfite intoxication disorders. This natural history study analyzed retrospective data for 58 living or deceased patients (MoCD‐A, n = 41; MoCD‐B, n = 17).
Ronen Spiegel +3 more
openaire +2 more sources