The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein subunit was crystallized using the hanging-drop technique, with PEG 4000 as precipitant. The crystals belong to space group P3112 or enantiomorph, with unit-cell parameters a = b = 171.0, c = 152.1 A. A solvent content of 75% was determined by a calibrated tetrachloromethane/toluene gradient which corresponds to three monomers per asymmetric unit. A 3 A resolution native data set was collected at beamline W32 of LURE, Orsay, France.
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Front Microbiol
July 2019
Center for Bioinformatics and Genome Biology, Fundación Ciencia y Vida, Santiago, Chile.
The ability to conserve energy in the presence or absence of oxygen provides a metabolic versatility that confers an advantage in natural ecosystems. The switch between alternative electron transport systems is controlled by the fumarate nitrate reduction transcription factor (FNR) that senses oxygen via an oxygen-sensitive [4Fe-4S] iron-sulfur cluster. Under O limiting conditions, FNR plays a key role in allowing bacteria to transition from aerobic to anaerobic lifestyles.
View Article and Find Full Text PDFMol Med Rep
December 2017
Department of Nephrology, The First Affiliated Hospital of Zhengzhou University, Zhengzhou, Henan 450052, P.R. China.
The reductase domains of neuronal NOS, endothelial NOS and two constitutive nitric oxide synthase (cNOS) share higher sequence similarity (>60%). In order to evaluate the role of ferredoxin‑NADP+ reductase (FNR) module in adjusting NOS catalytic activities, chimeras were by interchanging the FNR‑like module between endothelial NOS and neuronal NOS in the present study. The assays of steady‑state enzymatic activities for cytochrome c and ferricyanide reduction, NO synthesis and NADPH oxidation were performed spectrophotometrically.
View Article and Find Full Text PDFGenome Biol Evol
September 2013
Institute for Advanced Biosciences, Keio University, Tsuruoka, Japan.
The cAMP receptor protein (CRP)/fumarate and nitrate reduction regulatory protein (FNR)-type transcription factors (TFs) are members of a well-characterized global TF family in bacteria and have two conserved domains: the N-terminal ligand-binding domain for small molecules (e.g., cAMP, NO, or O(2)) and the C-terminal DNA-binding domain.
View Article and Find Full Text PDFInt J Food Microbiol
April 2009
USC2017 INRA Microbiologie de l'Environnement, IFR 146 ICORE, Université de Caen, Caen Cedex, France.
Ers has been identified in a recent study as a protein involved in the pathogenesis and the stress response of the lactic acid bacterium Enterococcus faecalis, an opportunistic pathogen. In the E. faecalis sequenced genome, Ers is annotated as a transcriptional regulator member of the Crp/Fnr family.
View Article and Find Full Text PDFBiochemistry
October 2007
Faculty of Life Sciences, University of Manchester, Manchester Interdisciplinary Biocentre, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Human methionine synthase reductase (MSR) is a 78 kDa flavoprotein that regenerates the active form of cobalamin-dependent methionine synthase (MS). MSR contains one FAD and one FMN cofactor per polypeptide and functions in the sequential transfer of reducing equivalents from NADPH to MS via its flavin centers. We report the 1.
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