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Reduction of fully oxidized Clostridium pasteurianum 8-Feox.,ox. ferredoxin by using pulse-radiolysis techniques yields the half-reduced species 8-Feox.,red. ferredoxin. The subsequent oxidation of 8-Feox.,red. ferredoxin with Co(NH3)5Cl2+ was studied. From a comparison with stopped-flow studies on the 2:1 Co(NH3)5Cl2+ oxidation of 8-Fered.,red. ferredoxin to the 8-Feox.,ox. form it is concluded that there is no redox co-operativity between the two 4-Fe centres in these reactions. ...

Ferredoxins [1] are a group of iron-sulfur proteins which mediate electron transfer in a wide variety of metabolic reactions. Ferredoxins can be divided into several subgroups depending upon the physiological nature of the iron-sulfur cluster(s). One of these subgroups are the 4Fe-4S ferredoxins, which are found in bacteria and which are thus often referred as bacterial-type ferredoxins. The structure of these proteins [2] consists of the duplication of a domain of twenty six amino acid residues; each of these domains contains four cysteine residues that bind to a 4Fe-4S center. Several structures of the 4Fe-4S ferredoxin domain have been determined (see for example ,PDB:1FDN,) [3]. The clusters consist of two interleaved 4Fe- and 4S-tetrahedra forming a cubane-like structure, in such a way that the four iron occupy the eight corners of a distorted cube. Each 4Fe-4S is attached to the polypeptide chain by four covalent Fe-S bonds involving cysteine residues. A number of proteins have been ...

The pea Ferredoxin-1 (Fed-1) gene encodes plastid-localized photosystem I ferredoxin. Its mRNA is perhaps the best-characterized nuclear-encoded transcript in plants that exhibits promoter-independent regulation of mRNA abundance (e.g., refs. 1 and 2). Fed-1 initially was identified in a cDNA screen for light-regulated mRNAs in pea (3) and was chosen for further study because Fed-1 mRNA accumulated faster than several other light-regulated mRNAs in etiolated pea seedlings exposed to light (4). Analysis of transgenic tobacco plants containing the transcribed sequence of the pea Fed-1 gene under the transcriptional control of the constitutive cauliflower mosaic virus 35S promoter (P35S) revealed that the light-regulated accumulation of Fed-1 mRNA was conferred by the mRNA sequence itself rather than by the promoter (1). Furthermore, the light effect on accumulation of Fed-1 mRNA transcribed from this chimeric gene was greater in green plants than in etiolated seedlings exposed to light for the ...

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InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

Burkholderia sp. RP007 aromatic 1,2-dioxygenase beta subunit (phnY),chloroplast-type ferredoxin (phnT2), catechol 2,3-dioxygenase (phnE2), and(phnX) genes, complete cds; and 2-hydroxymuconic semialdehyde dehydrogenase(phnG2) gene, partial ...

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SWISS-MODEL Template Library (SMTL) entry for 1fnb.1. REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2-PHOSPHO-5-AMP BOUND STATES

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.

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A mitochondrion-like organelle (MLO) was isolated from isotonic homogenates of Blastocystis. The organelle sedimented at 5000 g for 10 min, and had an isopycnic density in sucrose of 1.2 g ml−1. Biochemical characterization enabled the demonstration of several key enzymes that allowed the construction of a metabolic pathway consisting of an incomplete Krebs cycle linked to the oxygen-sensitive enzymes pyruvate : NADP+ oxidoreductase (PNO), acetate : succinate CoA transferase (ASCT) and succinate thiokinase (STK), which cumulatively are responsible for recycling CoA and generating ATP. The organelle differs from typical aerobic mitochondria in possessing an oxygen-sensitive PNO that can use FAD+ or FMN+ as electron acceptor but is inactive with NAD+, Spinacia oleracea ferredoxin or Clostridium pasteurianum ferredoxin. A gene with 77 % sequence similarity to the PNO mitochondrion precursor cluster from Euglena gracilis sp[Q941N5] was identified in the Blastocystis genome database. A second cluster with

1G3O: Azotobacter vinelandii ferredoxin I: a sequence and structure comparison approach to alteration of [4Fe-4S]2+/+ reduction potential

TY - JOUR. T1 - Photogeneration of NADPH by oligothiophenes coupled with ferredoxin- NADP reductase. AU - Kim, Y.. AU - Ikebukuro, K.. AU - Muguruma, H.. AU - Karube, I.. PY - 1998/1/3. Y1 - 1998/1/3. N2 - The photogeneration of nicotinamide adenine dinucleotide hydrophosphate (NADPH) and its associated reaction were studied in a novel photo-energy conversion system. The system was composed of the oligothiophene, dimethyl- 4,4-bipyridinium (MV2+), EDTA, and combined with ferredoxin-NADP reductase (FDR, E.C.1.18.1.2). The NADPH was generated by the FDR catalysis via the reduction of MV2+ by the photocatalysis of oligothiophene and EDTA as the sacrificial electron donor. As a result, the rate of the NADPH generation depended on the concentrations of nicotinamide adenine dinucleotide phosphate (NADP+) and MV2+. The effect of the intension of applied light showed the same tendency. Rate values of photoreduction of MV2+ and photogeneration of NADPH systems were investigated as a function of the ...

A flavoprotein (FAD). In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial [4Fe-4S] fe

Domain architectures containing the following SCOP superfamilies 55874,54211,56719 in Neisseria meningitidis 053442. Domain architectures illustrate each occurrence of 55874,54211,56719.

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Accepted name: 3-ketosteroid 9α-monooxygenase. Reaction: androsta-1,4-diene-3,17-dione + NADH + H+ + O2 = 9α-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O. Other name(s): KshAB; 3-ketosteroid 9α-hydroxylase. Systematic name: androsta-1,4-diene-3,17-dione,NADH:oxygen oxidoreductase (9α-hydroxylating). Comments: The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis. It is a two-component system consisting of a terminal oxygenase (KshA) and a ferredoxin reductase (KshB). The oxygenase contains a Rieske-type iron-sulfur center and non-heme iron. The reductase component is a flavoprotein containing an NAD-binding domain and a plant-type iron-sulfur cluster. The product of the enzyme is unstable, and spontaneously converts to 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: References:. 1. Petrusma, M., Dijkhuizen, L. and ...

Ferredoxins (Given) occurring generally in most microorganisms are small protein that make use of their iron-sulfur cluster to distribute electrons to various metabolic pathways likely including hydrogen creation. Fed2-Given9 encoded by genes in different ways governed by trophic circumstances are low-abundant protein that play prominent assignments in the tolerance to environmental strains. Regarding the selectivity/redundancy […]. ...

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I would view the second FeNi cluster on the right hand side as the potential origin of CODH/ACS, separated off in to the cytoplasm and of no further interest in the development of a proto-Ech. Ive flipped back on to a more normal orientation for the rest of the pictures as reading on one side does horrible things to my brain. In the next picture Ive got the first FeNi centre accepting low potential electrons from H2 at pH 10 and donating them, not to a structural FeS cluster as previously but to a ferredoxin, a soluble version of FeS, at pH 6 to give a an FeS moiety with a redox potential capable to reducing CO2 to CO, but in transportable form. Able to wander off elsewhere in the cytoplasm as the core power unit of the cell, to where ever CODH/ACS has ended up. Ferredoxin is one of the most ancient and simple peptides, possibly worth a post in its own right. Below shows the need for a low pH region close to the FeNi moiety to allow this conservation of reducing power ...

I would view the second FeNi cluster on the right hand side as the potential origin of CODH/ACS, separated off in to the cytoplasm and of no further interest in the development of a proto-Ech. Ive flipped back on to a more normal orientation for the rest of the pictures as reading on one side does horrible things to my brain. In the next picture Ive got the first FeNi centre accepting low potential electrons from H2 at pH 10 and donating them, not to a structural FeS cluster as previously but to a ferredoxin, a soluble version of FeS, at pH 6 to give a an FeS moiety with a redox potential capable to reducing CO2 to CO, but in transportable form. Able to wander off elsewhere in the cytoplasm as the core power unit of the cell, to where ever CODH/ACS has ended up. Ferredoxin is one of the most ancient and simple peptides, possibly worth a post in its own right. Below shows the need for a low pH region close to the FeNi moiety to allow this conservation of reducing power ...

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The enzyme from Burkholderia fungorum strain LB400 (previously Pseudomonas sp.) is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske- type iron-sulfur cluster and a catalytic mononuclear nonheme iron center. -!- Chlorine-substituted biphenyls can also act as substrates. -!- Similar to the three-component enzyme systems EC 1.14.12.3 and EC 1.14.12.11 ...

Butanol is currently one of the most discussed biofuels. Its use provides many benefits in comparison to bio-ethanol, but the price of its fermentative production is still high. Genetic improvements could help solve many problems associated with butanol production during ABE fermentation, such as its toxicity, low concentration achievable in the cultivation medium, the need for a relatively expensive substrate, and many more. Clostridium pasteurianum NRRL B-598 is non-type strain producing butanol, acetone, and a negligible amount of ethanol. Its main benefits are high oxygen tolerance, utilization of a wide range of carbon and nitrogen sources, and the availability of its whole genome sequence. However, there is no established method for the transfer of foreign DNA into this strain; this is the next step necessary for progress in its use for butanol production. We have described functional protocols for conjugation and transformation of the bio-butanol producer C. pasteurianum NRRL B-598 by foreign

5-Fluorouracil (5-FU) is a frequently used antitumor drug. Recently, it has been shown that mRNA and protein levels of the ferredoxin reductase gene (gene, FDXR; protein, FR) increase drastically after 5-FU treatment in various cell lines including colorectal cancer. The induction is mediated by p53 and enhanced reactive oxygen species (ROS)-associated apoptosis. Thus, knowledge about FDXR expression in human tissue and expression of the known splice variants is critical for understanding this finding. A sensitive and specific reverse transcriptase polymerase chain reaction (RT-PCR) assay for quantification of FDXR mRNA levels including the splice variants, a biological active variant (−18 bp) and an inactive variant (+18 bp), was developed and used to measure mRNAs after 5-FU chemotherapy in colorectal tissues of 40 cancer patients prior to and after treatment with 5-FU for 14 days. Before treatment, the great majority of normal tissues expressed the splice variants in a 100:1 ratio in favor ...

Formate is the major source of C1 units in many species of the genus Clostridium. In this study we have cloned and characterized the genes encoding pyruvate formate-lyase and its activating enzyme of Clostridium pasteurianum. The genetic and transcriptional organizations of the genes and the high le …

Order monoclonal and polyclonal Ferredoxin Reductase antibodies for many applications. Selected quality suppliers for anti-Ferredoxin Reductase antibodies.

Comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.3), an iron-sulfur oxygenase, and ferredoxin ...

Complete information for FDX1 gene (Protein Coding), Ferredoxin 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

On Jul 26, 2009, at 9:56 AM, Rowland McDonnell wrote: , P.S. You need to understand that a lot of your assumptions are wrong. , In particular, youve no idea the huge pain that Mac users go through , when trying to set up MacTeX if they want anything other than an , absolutely 100% standard installation - which you get by pressing the , `go button on the MacTeX installer. No interaction with the command , line or tlmgr or *ANYTHING* like that is needed - just install MacTeX, , fire up TeXShop, and theres a standard LaTeX setup which is all the , average Mac user can ever have now. Local variations are simple not , accessible to the average Mac user whos installed MacTeX. I have local variations installed in ~/Library/texmf. This has worked great with gwTeX and all releases of MacTeX to date. No pain at all, and this is what most Mac users do, as far as I know. -------------- next part -------------- A non-text attachment was scrubbed... Name: smime.p7s Type: application/pkcs7-signature ...

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Staphylococcus aureus; strain: COL; locus tag: SACOL1309 (SACOL_RS06680); product: 2-oxoglutarate ferredoxin oxidoreductase subunit beta

Metronidazole is taken up by anaerobes and then it is reduced to ferredoxin. This reduction will produce a toxic metabolite that kills anaerobes and protozoa ...

The transport of 99MoO42- into dinitrogen-fixing cells of Clostridium pasteurianum was investigated. Transport of molybdate in this organism is energy dependent; sucrose is required in the minimal media, and the system is inhibited by the glycolysis inhibitors, NaF, iodoacetic acid, and arsenate. The cells accumulate molybdate against a concentration gradient, and the uptake shows a marked dependence on temperature (optimum 37 C) and pH (optimum 6.0). The rate of molybdate uptake with increasing molybdate concentrations shows saturation kinetics with an apparent Km and Vmax of 4.8 X 10(-5) M and 55 nmol/g of dry cells per min, respectively. Inhibition studies with the anions SO42-, S2O32-, WO42-, and VO32- show that SO42- and WO42- competitively inhibit MoO42- uptake (apparent Ki [SO42-] is 3.0 X 10(-5) M; apparent Ki [WO42-] is 2.4 X 10(-5), whereas S2O32- and VO32- have no inhibitory effect. Exchange experiments with MoO42- show that only a small percentage of the 99MoO42- taken up by the ...

TY - JOUR. T1 - Mechanistic insights into Cu(I) cluster transfer between the chaperone CopZ and its cognate Cu(I)-transporting P-type ATPase, CopA. AU - Singleton, Chloe. AU - Hearnshaw, Stephen. AU - Zhou, Liang. AU - Le Brun, Nick. AU - Hemmings, Andrew. PY - 2009. Y1 - 2009. N2 - Multinuclear Cu(I) clusters are common in nature, but little is known about their formation or transfer between proteins. CopZ and CopA from Bacillus subtilis, which are involved in a copper-efflux pathway, both readily accommodate multinuclear Cu(I) clusters. Using the luminescence properties of a multinuclear Cu(I)-bound form of the two N-terminal soluble domains of CopA (CopAab) we have investigated the thermodynamic and kinetic properties of cluster formation and loss. We demonstrate that Cu(I)-bound forms of dimeric CopZ containing more than one Cu(I) per CopZ monomer can transfer Cu(I) to apo-CopAab, leading to the formation of luminescent dimeric CopAab. Kinetic studies demonstrated that transfer is a ...

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1.0 1.1 Brigle, KE et al. (1987) Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE and nifN, are structurally homologous to the products of the nitrogenase molybdenum-iron protein genes, nifD and nifK. J. Bacteriol. 169 1547-53 PubMed GONUTS page ...

mag:amb2922 K03738 aldehyde:ferredoxin oxidoreductase [EC:1.2.7.5] , (GenBank) Tungsten-containing aldehyde ferredoxin oxidoreductase (A) MSWTGKFLRIDLTNGSVKTEELNRAWARQYLGQRGLATKYFAEEVDPKVDPLSPANKMIF TTGPLTGTAASTGGRYSVVTKGPLTNCIACSNSGGFFGNELKNAGWDMIIVEGRSPKPVY LSIENETVEIRDAAEFWGKTVWETENGLKARHQDPMLRVATIGAAGEKGVLYACIVNDLH RAAGRSGVGAVMGSKNLKAIAVRGTRGVTVKDPDRFIKATIEQKKVLADNAVTGQGLPKY GTQVLMNVINEIGAMPTRNFKEVQFEGAHKISAEAMHEPRATDGKANLATNGACFGCTIA CGRISRMDPGHFSITSRPQYKEPSGGVEYEAAWAMGSDCGVDDLEACTFANFMCNEHGID PISFGSTLAAAMEMFEMGVITKEQTGGVELKFGSAEALVKMAELTGKGEGFGLELGQGSR RLCAKYGHPELSMTVKSQEFPAYDPRGIQGMGLTYATSNRGACHLRSYTVASEVLGIPFK SDPLATDGKAALVKAFQDATAAFDASGICIFTTFAWSLENLAPQIDAACEGEWTPEILLE VGERIWTLERQFNLAAGMTAADDTLPKRLLKDAAKTGPAKGLTSGLEKMLPEYYQLRGWT TDGVPTTETLKRLQLA ...

GenBank) porD pyruvate synthase subunit porD (EC 1.2.7.1) (pyruvate oxidoreductase delta chain) (pyruvate ferredoxin oxidoreductase ...

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