Faculty Opinions recommendation of LFR1 ferric iron reductase of Leishmania amazonensis is essential for the generation of infective parasite forms.

2015 ◽  
Author(s):  
Malcolm McConville
Keyword(s):  
Ferric Iron ◽  
Leishmania Amazonensis ◽  
Iron Reductase

Leishmania amazonensis ferric iron reductase (LFR1) is a bifunctional enzyme: Unveiling a NADPH oxidase activity

2019 ◽  
Vol 143 ◽  
pp. 341-353 ◽  
Author(s):  
N. Rocco-Machado ◽  
D. Cosentino-Gomes ◽  
M.T. Nascimento ◽  
L. Paes-Vieira ◽  
Y.A. Khan ◽  
...  
Keyword(s):  
Nadph Oxidase ◽  
Oxidase Activity ◽  
Ferric Iron ◽  
Leishmania Amazonensis ◽  
Bifunctional Enzyme ◽  
Nadph Oxidase Activity ◽  
Iron Reductase

scholarly journals Ferric iron reductase activity of LuxG from Photobacterium leiognathi

2016 ◽  
Vol 52 (4) ◽  
pp. 495-499 ◽  
Author(s):  
Eui Ho Lee ◽  
Ki Seok Nam ◽  
Seon Kwang Lee ◽  
Eugeney Oh ◽  
Chan Yong Lee
Keyword(s):  
Ferric Iron ◽  
Reductase Activity ◽  
Photobacterium Leiognathi ◽  
Iron Reductase

scholarly journals Biochemical characterization of Serpula lacrymans iron-reductase enzymes in lignocellulose breakdown

2019 ◽  
Vol 47 (1) ◽  
pp. 145-154 ◽  
Author(s):  
Irnia Nurika ◽  
Daniel C. Eastwood ◽  
Timothy D. H. Bugg ◽  
Guy C. Barker
Keyword(s):  
Ferric Iron ◽  
Biochemical Characterization ◽  
Recombinant Enzymes ◽  
Binding Domains ◽  
Lignin Decomposition ◽  
Pre Treatment ◽  
Serpula Lacrymans ◽  
Iron Reductase ◽  
Ir Genes

AbstractPutative iron-reductase (IR) genes from Serpula lacrymans with similarity to the conserved iron-binding domains of cellobiose dehydrogenase (CDH) enzymes have been identified. These genes were cloned and expressed to functionally characterize their activity and role in the decomposition of lignocellulose. The results show that IR1 and IR2 recombinant enzymes have the ability to depolymerize both lignin and cellulose, are capable of the reduction of ferric iron to the ferrous form, and are capable of the degradation of nitrated lignin. Expression of these genes during wheat straw solid-state fermentation was shown to correlate with the release of compounds associated with lignin decomposition. The results suggest that both IR enzymes mediate a non-enzymatic depolymerisation of lignocellulose and highlight the potential of chelator-mediated Fenton systems in the industrial pre-treatment of biomass.

scholarly journals Iron Reductase for Magnetite Synthesis in the Magnetotactic Bacterium Magnetospirillum magnetotacticum

1999 ◽  
Vol 181 (7) ◽  
pp. 2142-2147 ◽  
Author(s):  
Yasushi Noguchi ◽  
Taketomo Fujiwara ◽  
Katsuhiko Yoshimatsu ◽  
Yoshihiro Fukumori
Keyword(s):  
Ferric Iron ◽  
Reductase Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Flavin Mononucleotide ◽  
Homogeneous State ◽  
Magnetotactic Bacterium ◽  
Magnetospirillum Magnetotacticum ◽  
Iron Reductase

ABSTRACT Ferric iron reductase was purified from magnetotactic bacteriumMagnetospirillum (formerly Aquaspirillum)magnetotacticum (ATCC 31632) to an electrophoretically homogeneous state. The enzyme was loosely bound on the cytoplasmic face of the cytoplasmic membrane and was found more frequently in magnetic cells than in nonmagnetic cells. The molecular mass of the purified enzyme was calculated upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be about 36 kDa, almost the same as that calibrated by gel filtration analysis. The enzyme required NADH and flavin mononucleotide (FMN) as optimal electron donor and cofactor, respectively, and the activity was strongly inhibited by Zn2+ acting as a partial mixed-type inhibitor. TheKm values for NADH and FMN were 4.3 and 0.035 μM, respectively, and the Ki values for Zn2+ were 19.2 and 23.9 μM for NADH and FMN, respectively. When the bacterium was grown in the presence of ZnSO4, the magnetosome number in the cells and the ferric iron reductase activity declined in parallel with an increase in the ZnSO4 concentration of the medium, suggesting that the ferric iron reductase purified in the present study may participate in magnetite synthesis.

scholarly journals Acquisition, Transport, and Storage of Iron by Pathogenic Fungi

1999 ◽  
Vol 12 (3) ◽  
pp. 394-404 ◽  
Author(s):  
Dexter H. Howard
Keyword(s):  
Ferric Iron ◽  
Molecular Level ◽  
Pathogenic Fungi ◽  
Common Mechanism ◽  
Iron Starvation ◽  
Iron Assimilation ◽  
And Storage ◽  
Synthesis Regulation ◽  
Iron Reductase

Iron is required by most living systems. A great variety of means of acquisition, avenues of uptake, and methods of storage are used by pathogenic fungi to ensure a supply of the essential metal. Solubilization of insoluble iron polymers is the first step in iron assimilation. The two methods most commonly used by microorganisms for solubilization of iron are reduction and chelation. Reduction of ferric iron to ferrous iron by enzymatic or nonenzymatic means is a common mechanism among pathogenic yeasts. Under conditions of iron starvation, many fungi synthesize iron chelators known as siderophores. Two classes of compounds that function in iron gathering are commonly observed: hydroxamates and polycarboxylates. Two major responses to iron stress in fungi are a high-affinity ferric iron reductase and siderophore synthesis. Regulation of these two mechanisms at the molecular level has received attention. Uptake of siderophores is a diverse process, which varies among the different classes of compounds. Since free iron is toxic, it must be stored for further metabolic use. Polyphosphates, ferritins, and siderophores themselves have been described as storage molecules. The iron-gathering mechanisms used by a pathogen in an infected host are largely unknown and can only be posited on the basis of in vitro studies at present.

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