Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase

  title={Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase},
  author={Mk Chan and Swarnalatha Mukund and Arnulf Kletzin and M. W. W. Adams and D. C. Rees},
  pages={1463 - 1469}
The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100 degrees C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal form averaging. AOR consists of two identical subunits, each containing an Fe4S4 cluster and a molybdopterin-based tungsten cofactor that is analogous to the molybdenum… 

Purification and Molecular Characterization of the Tungsten-Containing Formaldehyde Ferredoxin Oxidoreductase from the Hyperthermophilic Archaeon Pyrococcus furiosus: the Third of a Putative Five-Member Tungstoenzyme Family

A third type of tungsten-containing enzyme, formaldehyde ferredoxin oxidoreductase (FOR), has now been characterized and is a homotetramer with a mass of 280 kDa and contains approximately 1 W atom, 4 Fe atoms, and 1 Ca atom per subunit, together with a pterin cofactor.

Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications.

Crystal structures of formaldehyde ferredoxin oxidoreductase (FOR), a tungstopterin-containing protein from the hyperthermophilic archaeon Pyrococcus furiosus, have been determined in the native

Purification and characterization of the tungsten enzyme aldehyde:ferredoxin oxidoreductase from the hyperthermophilic denitrifier Pyrobaculum aerophilum

Metal analysis and electron paramagnetic resonance (EPR) spectroscopy indicate that the P. aerophilum AOR contains one tungsten center and one [4Fe-4S]2+/1+ cluster per 68-kDa monomer, and the amino acid sequence has been identified using mass spectrometry.

An unprecedented function for a tungsten-containing oxidoreductase

Biochemical assays and product analysis confirmed that WOR5 is an aliphatic sulfonate ferredoxin oxidoreductase (ASOR), and a catalytic mechanism for ASOR is proposed based on the structural information and the potential role of ASOR in the cold-shock response is discussed.

The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus.

A structural comparison of AFEST with its mesophilic and thermophilic homologues, Brefeldin A esterase from Bacillus subtilis (BFAE) and EST2 from Alicyclobacillus acidocaldarius, reveals an increase in the number of intramolecular ion pairs and secondary structure content, as well as a significant reduction in loop extensions and ratio of hydrophobic to charged surface area.

Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum.

Structural comparison revealed that the presence of extensive hydrophobic interactions and a smaller cavity volume are likely to be the main factors contributing to the hyperthermostability of McoP.

The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures.

The Pyrococcus furiosus (PF) ornithine carbamoyltransferase (OTCase; EC is an extremely heat-stable enzyme that maintains about 50% of its activity after heat treatment for 60 min at 100

Characterization of an Aldehyde Oxidoreductase From the Mesophilic Bacterium Aromatoleum aromaticum EbN1, a Member of a New Subfamily of Tungsten-Containing Enzymes

AORAa appears to be a prototype of a new subfamily of bacterial AOR-like tungsten-enzymes, which differ from the previously known archaeal AORs mostly by their multi-subunit composition, their low sensitivity against oxygen, and the ability to use NAD+ as electron acceptor.

Tungstoenzymes: Occurrence, Catalytic Diversity and Cofactor Synthesis

Tungsten is the heaviest element used in biological systems. It occurs in the active sites of several bacterial or archaeal enzymes and is ligated to an organic cofactor (metallopterin or metal

Probing the role of oligomerization in the high thermal stability of Pyrococcus furiosus ornithine carbamoyltransferase by site-specific mutants.

Results suggest that extreme thermal stabilization of this OTCase is achieved in part through oligomerization, and all the variants show similar catalytic activities and kinetic properties when compared to the wild-type enzyme.



X‐ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus

The structures of the oxidized and reduced forms of the rubredoxin from the archaebacterium, Pyrococcus furiosus, an organism that grows optimally at 100 °C, have been determined by X‐ray

Structural and metabolic relationship between the molybdenum cofactor and urothione.

  • J. JohnsonK. Rajagopalan
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1982
The finding that urine samples from patients deficient in the molybdenum cofactor are devoid of urothione demonstrates a metabolic link between the two molecules, and a structural relationship is suggested.

Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii.

The crystal structure of the nitrogenase Fe-protein from Azotobacter vinelandii has been determined and it appears that interactions between the nucleotide and cluster sites must be indirectly coupled by allosteric changes occurring at the subunit interface.

Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms.

  • M. Adams
  • Biology
    FEMS microbiology reviews
  • 1994
Hyperthermophiles are a recently discovered group of microorganisms that grow at and above 90 degrees C and are thought to contain a new type of Entner-Doudoroff pathway for the conversion of carbohydrates ultimately to acetate, H2 and CO2.

Heat stability of a tetrameric enzyme, D-glyceraldehyde-3-phosphate dehydrogenase.

The tetrameric enzyme D-glyceraldehyde-3-phosphate dehydrogenase from the moderate thermophile Bacillus stearothermophilus is more stable to thermal denaturation than its counterpart from lobster muscle but changes in interactions at the surface appear to be equally important.