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Flavodoxin (0):
Recent article
Flavodoxin
Abstract
Kinetic intermediates that appear early during protein folding often resemble the relatively stable molten globule intermediates formed by several proteins under mildly denaturing conditions. Molten globules have a substantial amount of secondary structure but lack virtually all tertiary side-chain...
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PMID: 19959481
PDF is available here.
PDF is available here.
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Biochimica et Biophysica Acta (1797)2 2010
Abstract
I (PSI) to Ferredoxin-NADP(+) reductase (FNR). A number of Anabaena Fld (AnFld) variants with replacements at the interaction surface with FNR and PSI indicated that neither polar nor hydrophobic residues resulted critical for the interactions, particularly with FNR. This suggests that the solvent e...
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PMID: 19900400
PDF is available here.
PDF is available here.
Abstract
Environmental stresses - especially drought and salinity - and iron limitation are the primary causes of crop yield losses. Therefore, improvement of plant stress tolerance has paramount relevance for agriculture, and vigorous efforts are underway to design stress-tolerant crops. Thr...
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PMID: 21415892
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (284)30 2009
Abstract
Biophysical Journal (96)2 2009
Abstract
We investigated the folding energy landscape of an alpha/beta protein, apoflavodoxin, in the presence of inert macromolecular crowding agents, using in silico and in vitro approaches. By means of coarse-grained molecular simulations and topology-based potential interactions, we probed the effects of...
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PMID: 19167312
PDF is available here.
PDF is available here.
Abstract
Detailed information about unfolded states is required to understand how proteins fold. Knowledge about folding intermediates formed subsequently is essential to get a grip on pathological aggregation phenomena. During folding of apoflavodoxin, which adopts the widely prevalent α−β parallel topol...
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PMID: 19053416
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)41 2008
Abstract
To understand how proteins fold in vivo, it is important to investigate the effects of macromolecular crowding on protein folding. Here, the influence of crowding on in vitro apoflavodoxin folding, which involves a relatively stable off-pathway intermediate with molten globule characteristics, is re...
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PMID: 18640986
PDF is available here.
PDF is available here.
Abstract
We report that NrdI is a flavodoxin counterpart to YfaE for the class Ib RNR. It possesses redox properties unprecedented for a flavodoxin (E(ox/sq) = -264 +/- 17 mV and E(sq/hq) = -255 +/- 17 mV) that allow it to mediate a two-electron reduction of the diferric cluster of NrdF via two successive on...
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PMID: 18799738
PDF is available here.
PDF is available here.
Biophysical Journal (95)5 2008
Abstract
Submolecular details of Azotobacter vinelandii apoflavodoxin (apoFD) (un)folding are revealed by time-resolved fluorescence anisotropy using wild-type protein and variants lacking one or two of apoFD's three tryptophans. ApoFD equilibrium (un)folding by guanidine hydrochloride follows a three-state...
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PMID: 18708472
PDF is available here.
PDF is available here.
Abstract
We have modeled here the interactions between FNR and both of its protein partners, Fd and Fld, using surface energy analysis, computational rigid-body docking simulations, and interface side-chain refinement. The results, consistent with previous experimental data, suggest the existence of alternat...
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PMID: 18260112
PDF is available here.
PDF is available here.
Biophysical Journal (95)4 2008
Abstract
Partly unfolded protein conformations close in energy to the native state may be involved in protein functioning and also be related to folding diseases, but yet their structure and energetics are poorly understood. One such conformation, the monomeric and well-behaved molten globule of Helicobacter...
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PMID: 18441031
PDF is available here.
PDF is available here.
Abstract
A small contraction concomitant with the relaxation of the protein in ca. 3 μs is observed upon ns-laser excitation at 455 nm of the Cys69Ala (C69A) mutant of flavodoxin II from Azotobacter vinelandii. This constitutes another example of detection of a UV–vis silent transient species through a pho...
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PMID: 18643903
PDF is available here.
PDF is available here.
Journal of Bacteriology (190)14 2008
Abstract
We show that both clusters are expressed simultaneously as two independent operons. The NrdEF enzyme is functionally active in vitro, while the NrdE*F* enzyme is not. The NrdF* protein lacks three of the six highly conserved iron-liganding side chains and cannot form a dinuclear iron site or a tyros...
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PMID: 18502861
PDF is available here.
PDF is available here.
Abstract
We show that monovalent cations in biologically relevant amounts have dramatic effects on apoflavodoxin stability. The effect is largest for Gdm(+) and decreases as a function of increased cation charge density (Gdm(+)>NH(4)(+)K(+) approximately Cs(+) approximately Na(+)>Li(+)). A linear correlation...
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PMID: 18342618
PDF is available here.
PDF is available here.
Biochemistry (Washington) (47)15 2008
Abstract
The redox potential of the flavin mononucleotide (FMN) hydroquinones for one-electron reduction in the Desulfovibrio vulgaris ( D. vulgaris) flavodoxin ( E sq/hq for FMNH (*)/FMNH (-)) was calculated using the crystal structure of the relevant hydroquinone form and compared to the results of the Clo...
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PMID: 18355044
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)13 2008
Abstract
We have now established that purified CYP170A1 carries out two sequential allylic oxidations to convert epi-isozizaene to an epimeric mixture of albaflavenols and thence to the sesquiterpene antibiotic albaflavenone. Gas chromatography/mass spectrometry analysis of S. coelicolor culture extracts est...
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PMID: 18234666
PDF is available here.
PDF is available here.
Abstract
We report the conformational stability of the protein in neutral and acidic pH. The apoprotein remains native between pH 12 and 5 and adopts a monomeric molten globule conformation at more acidic pH values. The equilibrium unfolding in urea appears two-state for either conformation, but the native o...
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PMID: 17998211
PDF is available here.
PDF is available here.
Journal of Bacteriology (190)3 2008
Abstract
I subunits) was disrupted or deleted. Each of the nuo mutants will not grow in amino acid-based medium unless supplemented with an alternative respiratory substrate such as formate. Unlike the nuo genes, Cj1574c is an essential gene and could not be disrupted unless an intact copy of the gene was pr...
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PMID: 18065531
PDF is available here.
PDF is available here.
Abstract
I (PSI), and its electron acceptor, ferredoxin-NADP+ reductase (FNR), were analyzed. Trp57, Ile59, and Ile92 contributed to the optimal orientation and tightening of the FNR:Fld and PSI:Fld complexes. However, these side chains did not appear to be involved in crucial specific interactions, but rath...
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PMID: 18177021
PDF is available here.
PDF is available here.
Abstract
We are exploring to screen for novel inhibitory compounds is to perform thermal upshift assays, for which a detailed knowledge of protein thermostability and cofactor binding properties is of great help. However, very little is known on the stability and ligand binding properties of H. pylori flavod...
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PMID: 18095659
PDF is available here.
PDF is available here.
Methods in Enzymology (437) 2008
Abstract
Crystallographic studies on flavodiiron proteins (FDPs) have revealed that the common sequence core ( approximately 400 residues) that defines this protein family comprises two structural domains. The N-terminal domain (of approximately 250 residues) displays a metallo-beta-lactamase-like-fold, bein...
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PMID: 18433620
PDF is available here.
PDF is available here.
Abstract
We performed a combined experimental and computational study on the 148-residue single-domain alpha/beta protein, Desulfovibrio desulfuricans apoflavodoxin. In vitro thermal unfolding experiments, as well as assessment of native and denatured structures, were probed by using far-UV CD in the presenc...
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PMID: 18024596
PDF is available here.
PDF is available here.
Abstract
We report here the X-ray structure of the apoflavodoxin from the pathogen Helicobacter pylori. The protein naturally lacks one of the conserved aromatic residues that close the isoalloxazine pocket in Anabaena, and the structure has been determined in a medium lacking phosphate. In spite of these si...
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PMID: 17623845
PDF is available here.
PDF is available here.
Abstract
Our data indicate that the side chain of position 57 does not modulate E(ox/sq) by aromatic stacking or solvent exclusion, but rather by influencing the relative strength of the H-bond between the N(5) of the flavin and the Asn58-Ile59 bond. A correlation was observed between the isoalloxazine incre...
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PMID: 17904516
PDF is available here.
PDF is available here.
FEBS Letters (581)26 2007
Abstract
We show that increased amount of secondary structure is acquired in the folded states of two structurally-different proteins (alpha-helical VlsE and alpha/beta flavodoxin) in the presence of macromolecular crowding agents. The structural content of flavodoxin and VlsE is enhanced by 33% and 70%, res...
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PMID: 17919600
PDF is available here.
PDF is available here.
FEMS Microbiology Letters (275)1 2007
Abstract
In Clostridium acetobutylicum, [FeFe]-hydrogenase is involved in hydrogen production in vivo by transferring electrons from physiological electron donors, ferredoxin and flavodoxin, to protons. In this report, by modifications of the purification procedure, the specific activity of the enzyme has be...
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PMID: 17681007
PDF is available here.
PDF is available here.
Protein Science (16)10 2007
Abstract
The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multime...
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PMID: 17893367
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (282)35 2007
Abstract
The flavin mononucleotide (FMN) quinones in flavodoxin have two characteristic redox potentials, namely, Em(FMNH./FMNH-) for the one-electron reduction of the protonated FMN (E1) and Em(FMN/FMNH.) for the proton-coupled one-electron reduction (E2). These redox potentials in native and mutant flavodo...
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PMID: 17602164
PDF is available here.
PDF is available here.
Abstract
Iron limitation affects one-third of the cultivable land on Earth and represents a major concern for agriculture. It causes decline of many photosynthetic components, including the Fe-S protein ferredoxin (Fd), involved in essential oxidoreductive pathways of chloroplasts. In cyanobacteria and some...
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PMID: 17592141
PDF is available here.
PDF is available here.
Journal of Bacteriology (189)13 2007
Abstract
We found that the flavin mononucleotide in the flavodoxin of Helicobacter pylori is degraded to riboflavin via the phosphomonoesterase activity of class C acid phosphatase. The result is a conversion of holoflavodoxin to apoflavodoxin....
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PMID: 17449605
PDF is available here.
PDF is available here.
Journal of Bacteriology (189)13 2007
Abstract
We show that fqrB (HP1164), which is essential and highly conserved among the epsilonproteobacteria, exhibits NADPH oxidoreductase activity. FqrB was purified by nickel interaction chromatography following overexpression in Escherichia coli. The protein contained flavin adenine dinucleotide and exhi...
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PMID: 17468253
PDF is available here.
PDF is available here.
Biochimica et Biophysica Acta (1774)7 2007
Abstract
Our results illustrate the prospects of FAD conjugates in sensitive detection of progesterone in biological matrices in a biosensor based on the recombination of apoGOx with progesterone-conjugated FAD....
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PMID: 17544346
PDF is available here.
PDF is available here.
Abstract
This paper proposes a parameterized polynomial time approximation scheme (PTAS) for aligning two protein structures, in the case where one protein structure is represented by a contact map graph and the other by a contact map graph or a distance matrix. If the sequential order of alignment is not re...
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PMID: 17683261
PDF is available here.
PDF is available here.
Detoxification of 2,4-dinitrotoluene by transgenic tobacco plants expressing a bacterial flavodoxin.
Abstract
We have explored the possibility of overcoming the phytotoxicity of the highly toxic and recalcitrant nitroderivative 2,4-dinitrotoluene (2,4-DNT) by expressing a cyanobacterial flavodoxin (Fld) in tobacco plants. We demonstrate here that transformants accumulating Fld in plastids display a remarkab...
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PMID: 17612192
PDF is available here.
PDF is available here.
Journal of Physical Chemistry B (111)20 2007
Abstract
We also analyzed the observed values of ln k(ET) with Marcus theory, but could not obtain reasonable results. Our analysis suggests that the average distance, rather than the shortest (edge to edge) distance or interplanar angles between the aromatics rings, is the key factor in the process of the p...
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PMID: 17474766
PDF is available here.
PDF is available here.
Abstract
The standard Karplus equation for calculating 3J coupling constants from any given dihedral angle requires three empirical coefficients be determined that relate to the magnitudes of three modes of the angle dependency of 3J. Considering cosine modes only (bimodal, unimodal and baseline component),...
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PMID: 17333486
PDF is available here.
PDF is available here.
Abstract
A Synechococcus sp. strain PCC 7002 Fe bioreporter was constructed containing the isiAB promoter fused to the Vibrio harveyi luxAB genes. Bioreporter luminescence was characterized with respect to the free ferric ion concentration in trace metal-buffered synthetic medium. The applicability of the Fe...
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PMID: 17158623
PDF is available here.
PDF is available here.
Abstract
We tested the ability of two Bacillus subtilis flavodoxins (YkuN and YkuP) to support catalysis by purified B. subtilis NOS (bsNOS). When an NADPH-utilizing bacterial flavodoxin reductase (FLDR) was added to reduce YkuP or YkuN, both supported NO synthesis from either L-arginine or N-hydroxyarginine...
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PMID: 17127770
PDF is available here.
PDF is available here.
Iubmb Life (59)4-5 2007
Abstract
Flavodoxins (Flds) are mobile electron carriers containing flavin mononucleotide as the prosthetic group. They are isofunctional with the ubiquitous electron shuttle ferredoxin (Fd), mediating essentially the same redox processes among a promiscuous lot of donors and acceptors. While Fds are distrib...
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PMID: 17505975
PDF is available here.
PDF is available here.
Biophysical Chemistry (124)2 2006
Abstract
We need fast and accurate evolutionary models which can analyze the effects of selection, drift and fixation of a protein sequence in a population that are grounded by physical parameters governing the folding and binding properties of the sequence. In this study, various knowledge-based, force fiel...
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PMID: 16837122
PDF is available here.
PDF is available here.
Abstract
We demonstrate that FldHQ makes [Fe4S4]0 Av2, which is sufficiently characterized to demonstrate unique physical properties that distinguish it from the previously characterized Ti(III)-reduced [Fe4S4]0 Av2. In particular, Evans NMR magnetic susceptibility and EPR measurements indicate that FldHQ-re...
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PMID: 17085583
PDF is available here.
PDF is available here.
Abstract
We have exploited E. coli flavodoxin containing non-covalently bound flavin mononucleotide (FMN) as a model substrate for monitoring protein degradation. It was found that FtsH degrades FMN-free apo-flavodoxin but not holo-flavodoxin. However, degradation of a mutant flavodoxin carrying a substituti...
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PMID: 16563797
PDF is available here.
PDF is available here.
Abstract
The development of lysine 2,3-aminomutase as a robust biocatalyst hinges on the development of an in vivo activation system to trigger catalysis. This is the first report to show that, in the absence of chemical reductants, lysine 2,3-aminomutase activity is dependent upon the presence of flavodoxin...
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PMID: 16957271
PDF is available here.
PDF is available here.
Abstract
The predominant equilibrium in proteins is not between native and unfolded states, it is between the native and multiple partially unfolded forms. Some of these partially unfolded forms can be energetically close to the native state and, therefore, have the potential to become appreciably populated....
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PMID: 16870449
PDF is available here.
PDF is available here.
Abstract
The energetics of alpha-helix formation are fairly well understood and the helix content of a given amino acid sequence can be calculated with reasonable accuracy from helix-coil transition theories that assign to the different residues specific effects on helix stability. In internal helical positi...
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PMID: 16755589
PDF is available here.
PDF is available here.
Plant Cell Online (18)8 2006
Abstract
We report here that chloroplast Fd also declined in plants exposed to oxidants or stress conditions. A purified cyanobacterial Fld was able to mediate plant Fd-dependent reactions in vitro, including NADP+ and thioredoxin reduction. Tobacco (Nicotiana tabacum) plants expressing Fld in chloroplasts d...
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PMID: 16829589
PDF is available here.
PDF is available here.
Protein Science (15)8 2006
Abstract
We report here 17 apoflavodoxin large-to-small mutations that cause overall protein destabilizations of 0.6-3.9 kcal.mol(-1). By comparing two-state urea and three-state thermal unfolding data, the overall destabilizations observed are partitioned into effects on the N-to-I and on the I-to-U equilib...
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PMID: 16877708
PDF is available here.
PDF is available here.
Abstract
We here assess the kinetic folding/binding landscape for Desulfovibrio desulfuricans flavodoxin that coordinates an FMN cofactor. The apo-form folds in a two-step process involving a burst-phase intermediate. Studies on Tyr98Ala and Trp60Ala variants reveal that these aromatics-that stack with the F...
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PMID: 16730634
PDF is available here.
PDF is available here.
Journal of Molecular Biology (359)3 2006
Abstract
We present a comprehensive Phi-value analysis to characterize the structure of its transition state. A total of 34 non-disruptive mutations are made throughout the structure and a range of Phi-values from zero to one are observed. In addition, a small set of eight aliphatic small-to-large mutations...
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PMID: 16647718
PDF is available here.
PDF is available here.
Current Biology (16)11 2006
Abstract
We propose that the localization of Agg2p and Agg3p to the proximal region of the flagella may be important for interpreting light signals....
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PMID: 16753570
PDF is available here.
PDF is available here.
Abstract
The Fur (ferric uptake regulator) protein is a global regulator in most prokaryotes that controls a large number of genes. Fur is a classical repressor that uses ferrous iron as co-repressor and binds to specific DNA sequences (iron boxes) as a dimer. Three different genes coding for Fur homologues...
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PMID: 16799864
PDF is available here.
PDF is available here.
Abstract
We have analyzed in detail the stability of the apoflavodoxin from Anabaena PCC 7119 and the energetics of its functional complex with FMN. Here, we use the Anabaena holoprotein to directly investigate the contribution of the bound cofactor to protein stability through a detailed analysis of the che...
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PMID: 16444751
PDF is available here.
PDF is available here.
Journal of Molecular Biology (358)3 2006
Abstract
We study the folding landscapes of three proteins from the flavodoxin family (CheY, apoflavodoxin, and cutinase) using a simple nucleation and growth model that accurately describes both experimental and simulation results for the transition state structure, and the structure of on-pathway and misfo...
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PMID: 16563435
PDF is available here.
PDF is available here.
Journal of Molecular Biology (358)3 2006
Abstract
We have filled three small cavities in apoflavodoxin and determined by NMR and equilibrium unfolding analysis their impact in protein structure and stability. The smallest cavity (14 A3) has been filled, at two different positions, with a variety of residues and, in all cases, the mutant proteins ar...
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PMID: 16563433
PDF is available here.
PDF is available here.
Microbiology (152)Pt 4 2006
Abstract
The NADP(H)-dependent enzymes glucose-6-phosphate dehydrogenase (G6PDH) and ferredoxin(flavodoxin)-NADP(H) reductase (FPR), encoded by the zwf and fpr genes, respectively, are committed members of the soxRS regulatory system involved in superoxide resistance in Escherichia coli. Exposure of E. coli...
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PMID: 16549675
PDF is available here.
PDF is available here.
Abstract
Flavodoxins are electron-transfer proteins involved in a variety of photosynthetic and non-photosynthetic reactions in bacteria, whereas, in eukaryotes, a descendant of the flavodoxin gene helps build multidomain proteins. The redox activity of flavodoxin derives from its bound flavin mononucleotide...
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PMID: 16465441
PDF is available here.
PDF is available here.
Abstract
In this work the catalytic properties of a cytochrome P450 immobilised onto an electrode surface are improved by means of the molecular Lego approach.
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PMID: 16538250
PDF is available here.
PDF is available here.
Abstract
Many native proteins occasionally form partially unfolded forms (PUFs), which can be detected by hydrogen/deuterium exchange and NMR spectroscopy. Knowledge about these metastable states is required to better understand the onset of folding-related diseases. So far, not much is known about where PUF...
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PMID: 16537490
PDF is available here.
PDF is available here.
Genes to Cells (11)3 2006
Abstract
We have found that FtsH degrades E. coli apo-flavodoxin (apo-Fld) but not holo-Fld containing non-covalently bound flavin mononucleotide (FMN). A mutant Fld carrying a substitution of Tyr94 to Asp (Fld(YD)) with a lower affinity for FMN was efficiently degraded by FtsH. To elucidate the directionali...
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PMID: 16483314
PDF is available here.
PDF is available here.
Analytical Biochemistry (350)1 2006
Abstract
A method for fluorescence detection of a protein's redox state based on resonance energy transfer from an attached fluorescence label to the prosthetic group of the redox protein is described and tested for proteins containing three types of prosthetic groups: a type-1 copper site (azurin, amicyanin...
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PMID: 16430854
PDF is available here.
PDF is available here.