Results 1 to 10 of about 70 (55)
Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2007 The tungsten–iron–sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a
Oliver Einsle +2 more
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Direct Electrochemistry of Molybdenum and Tungsten Enzymes [PDF]
, 2018 Molybdenum and tungsten enzymes are almost omnipresent in living organisms; they catalyze a large variety of reactions on a large range of substrates, and are involved in a number of key cellular functions, like bacterial respiration, carbon, sulfur, and nitrogen cycles, and detoxification.
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Obligately Tungsten-Dependent Enzymes─Catalytic Mechanisms, Models and Applications
BiochemistryTungsten-dependent enzymes incorporate a tungsten ion into their active site in the form of a complex with two pyranometallopterin (MPT) molecules, also known as tungsten cofactor (W-co). W-co-containing enzymes are found in several bacteria and archaea, predominantly in enzymes involved in anaerobic metabolism.
Johann Heider, Maciej Szaleniec
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Molybdenum and tungsten enzymes redox properties – A brief overview
Coordination Chemistry Reviews, 2019 Abstract Metalloproteins and metal-containing enzymes are well known to be essential to life. Molybdenum and tungsten are the heaviest transition metals used by biology. The mononuclear molybdenum (and tungsten) containing enzymes have in common a particular conserved metal centre (Mo, W) coordinated by one or two pyranopterins.
José J. G. Moura, Cristina M. Cordas
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Bond Valence Sum Parameters for Analyzing Pyranopterin Tungsten Enzyme Structures
MoleculesThe determination of tungsten oxidation states and W–ligand bond lengths for pyranopterin tungsten enzymes can be negatively impacted by Fourier series termination effects and photodamage/photoreduction in the X-ray beam. As a result, a new set of bond valence sum (BVS) parameters have been derived from bond length data on W(+4) and W(+6) model ...
Martin L Kirk, Jesse Lepluart
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Pyranopterin conformation defines the function of molybdenum and tungsten enzymes [PDF]
Proceedings of the National Academy of Sciences, 2012 We have analyzed the conformations of 319 pyranopterins in 102 protein structures of mononuclear molybdenum and tungsten enzymes. These span a continuum between geometries anticipated for quinonoid dihydro, tetrahydro, and dihydro oxidation states. We demonstrate that pyranopterin conformation is correlated with the protein folds defining the three ...
Richard A, Rothery +4 more
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The Use of Tungsten in Potentiometry to Detect Pospat Baffer and Urease Enzyme [PDF]
Jurnal Penelitian Pendidikan IPA, 2021 This study aims to characterize phosphate buffer and urease enzymes through the absorbance spectrum of UV-Vis and FTIR using tungsten as the indicator electrode. The method used in this research is the biosensor potentiometric method carried out in the Laboratory of the Faculty of Mathematics and Natural Sciences, State University of Medan and the ...
Victor H Sihombing, Abd Hakim S
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Exploring the Active Site of the Tungsten, Iron-Sulfur Enzyme Acetylene Hydratase [PDF]
Journal of Bacteriology, 2011 ABSTRACT The soluble tungsten, iron-sulfur enzyme acetylene hydratase (AH) from mesophilic Pelobacter acetylenicus is a member of the dimethyl sulfoxide (DMSO) reductase family. It stands out from its class as it catalyzes a nonredox reaction, the addition of H 2 O to acetylene (H—C≡
Schink, Bernhard +2 more
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Molybdenum Incorporation in Tungsten Aldehyde Oxidoreductase Enzymes from Pyrococcus furiosus [PDF]
Journal of Bacteriology, 2010 ABSTRACT The hyperthermophilic archaeon Pyrococcus furiosus expresses five aldehyde oxidoreductase (AOR) enzymes, all containing a tungsto-bispterin cofactor. The growth of this organism is fully dependent on the presence of tungsten in the growth medium.
Sevcenco, A.M. (author) +7 more
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Transition metal sulfur chemistry and its relvance to molybdenum and tungsten enzymes [PDF]
Journal of Inorganic Biochemistry, 1997 Abstract
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