Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity [PDF]
The journal of biological chemistry, American Society for
Biochemistry and Molecular Biology, 2000, 275, pp.115-21, 2014 Desulfoferrodoxin is a small protein found in sulfate-reducing bacteria that contains two independent mononuclear iron centers, one ferric and one ferrous. Expression of desulfoferrodoxin from Desulfoarculus baarsii has been reported to functionally complement a superoxide dismutase deficient Escherichia coli strain.
arxiv +1 more source
Hydrogen bonding to the cysteine ligand of superoxide reductase: acid--base control of the reaction intermediates [PDF]
Journal of biological inorganic chemistry : JBIC : a publication
of the Society of Biological Inorganic Chemistry, 2013, 18, pp.815 - 830, 2015 Superoxide reductase SOR is a non-heme iron metalloenzyme that detoxifies superoxide radical in microorganisms. Its active site consists of an unusual non-heme Fe2+ center in a [His4 Cys1] square pyramidal pentacoordination, with the axial cysteine ligand proposed to be an essential feature in catalysis.
arxiv +1 more source
Enzymatic AND Logic Gates Operated Under Conditions Characteristic of Biomedical Applications [PDF]
J. Phys. Chem. B 114, 12166-12174 (2010), 2010 Experimental and theoretical analyses of the lactate dehydrogenase and glutathione reductase based enzymatic AND logic gates in which the enzymes and their substrates serve as logic inputs are performed. These two systems are examples of the novel, previously unexplored, class of biochemical logic gates that illustrate potential biomedical applications
arxiv +1 more source
Virus-Encoded Ribonucleotide Reductases [PDF]
arXiv, 2014 Ribonucleotide reductases are encoded by many viruses, but without other enzymes of nucleotide metabolism of no obvious use. A look at the enzymes' molecular properties and their possible mutator action may give clues.
arxiv
Reaction of the NAD(P)H:flavin oxidoreductase from Escherichia coli with NADPH and riboflavin: identification of intermediates [PDF]
Biochemistry, American Chemical Society, 1998, 37, pp.11879-87, 2014 Flavin reductase catalyzes the reduction of free flavins by NAD(P)H. As isolated, Escherichia coli flavin reductase does not contain any flavin prosthetic group but accommodates both the reduced pyridine nucleotide and the flavin substrate in a ternary complex prior to oxidoreduction.
arxiv
Allosteric communication in Dihydrofolate Reductase: Signaling network and pathways for closed to occluded transition and back [PDF]
arXiv, 2007 E. Coli. dihydrofolate reductase (DHFR) undergoes conformational transitions between the closed (CS) and occluded (OS) states which, respectively, describe whether the active site is closed or occluded by the Met20 loop. A sequence-based approach is used to identify a network of residues that represents the allostery wiring diagram.
arxiv
Surface modified sulfur nanoparticles can escape the glutathione reductase mediated detoxification system in fungi [PDF]
arXiv, 2015 The antifungal effects of orthorhombic (~10 nm; spherical) and monoclinic (~50 nm; tetrapod) sulfur nanoparticles (SNPs) were studied against the NADPH-dependent glutathione reductase (GR) mediated xenobiotic detoxification system (GSH-GSSG) in filamentous fungi (Aspergillus niger as a model organism).
arxiv
The di-flavoenzyme reductase directly activates oxygen for the metabolism of diverse drug molecules by liver microsomal Cytochrome P450s [PDF]
arXiv, 2006 This submission has been withdrawn by arXiv administration due to complaints of misuse of institutional affiliation.
arxiv
A Random Force is a Force, of Course, of Coarse: Decomposing Complex Enzyme Kinetics with Surrogate Models [PDF]
, 2009 The temporal autocorrelation (AC) function associated with monitoring order parameters characterizing conformational fluctuations of an enzyme is analyzed using a collection of surrogate models. The surrogates considered are phenomenological stochastic differential equation (SDE) models. It is demonstrated how an ensemble of such surrogate models, each
arxiv +1 more source
Superoxide reductase from Desulfoarculus baarsii [PDF]
Methods in Enzymology, Elsevier, 2001, 349, pp.123-9, 2014 Superoxide radical (O2.-) is the univalent reduction product of molecular oxygen and belongs to the group of the so-called toxic oxygen derivatives. For years the only enzymatic system known to catalyze the elimination of superoxide was the superoxide dismutase (SOD), which catalyzes dismutation of superoxide radical anions to hydrogen peroxide and ...
arxiv