Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A genus of gram-positive, anaerobic, coccoid bacteria that is part of the normal flora of the mouth, upper respiratory tract, and large intestine in humans. Its organisms cause infections of soft tissues and bacteremias.
An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.
An iron-sulfur protein which serves as an electron carrier in enzymatic steroid hydroxylation reactions in adrenal cortex mitochondria. The electron transport system which catalyzes this reaction consists of adrenodoxin reductase, NADP, adrenodoxin, and cytochrome P-450.
A plant genus of the family SOLANACEAE after which the compound SCOPOLAMINE HYDROBROMIDE got its name.
A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.
A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.
A genus of gram-negative, ovoid to rod-shaped bacteria that is phototrophic. All species use ammonia as a nitrogen source. Some strains are found only in sulfide-containing freshwater habitats exposed to light while others may occur in marine, estuarine, and freshwater environments.
An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
A plant genus of the family SOLANACEAE. Members contain TROPANES. The common name of trumpet flower is also sometimes used for GELSEMIUM.
A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
A plant genus of the family SOLANACEAE which contains TROPANES.
A genus of gram-negative, aerobic bacteria found in soil and water. Its organisms occur singly, in pairs or irregular clumps, and sometimes in chains of varying lengths.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A plant genus of the family SOLANACEAE. Members contain CEREBROSIDES and SCOPOLETIN.
A phylum of oxygenic photosynthetic bacteria comprised of unicellular to multicellular bacteria possessing CHLOROPHYLL a and carrying out oxygenic PHOTOSYNTHESIS. Cyanobacteria are the only known organisms capable of fixing both CARBON DIOXIDE (in the presence of light) and NITROGEN. Cell morphology can include nitrogen-fixing heterocysts and/or resting cells called akinetes. Formerly called blue-green algae, cyanobacteria were traditionally treated as ALGAE.
A plant species of the genus ATROPA, family SOLANACEAE that contains ATROPINE; SCOPOLAMINE; BELLADONNA ALKALOIDS and other SOLANACEOUS ALKALOIDS. Some species in this genus are called deadly nightshade which is also a common name for SOLANUM.
An order of CRENARCHAEOTA consisting of aerobic or facultatively aerobic, chemolithotrophic cocci which are extreme thermoacidophiles. They lack peptidoglycan in their cell walls.
Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
Stable iron atoms that have the same atomic number as the element iron, but differ in atomic weight. Fe-54, 57, and 58 are stable iron isotopes.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
A genus of gram-negative, anaerobic, rod-shaped bacteria capable of reducing sulfur compounds to hydrogen sulfide. Organisms are isolated from anaerobic mud of fresh and salt water, animal intestines, manure, and feces.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Solution titration in which the end point is read from the electrode-potential variations with the concentrations of potential determining ions. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Dithionite. The dithionous acid ion and its salts.
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes.
An enzyme that catalyzes the formation of 2 molecules of glutamate from glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 1.4.1.13.
Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
A genus of facultatively anaerobic heterotrophic archaea, in the order THERMOPLASMALES, isolated from self-heating coal refuse piles and acid hot springs. They are thermophilic and can grow both with and without sulfur.
One of the three domains of life (the others being BACTERIA and ARCHAEA), also called Eukarya. These are organisms whose cells are enclosed in membranes and possess a nucleus. They comprise almost all multicellular and many unicellular organisms, and are traditionally divided into groups (sometimes called kingdoms) including ANIMALS; PLANTS; FUNGI; and various algae and other taxa that were previously part of the old kingdom Protista.
The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Vibrio- to spiral-shaped phototrophic bacteria found in stagnant water and mud exposed to light.
An enzyme system that catalyzes the fixing of nitrogen in soil bacteria and blue-green algae (CYANOBACTERIA). EC 1.18.6.1.
An enzyme found in bacteria. It catalyzes the reduction of FERREDOXIN and other substances in the presence of molecular hydrogen and is involved in the electron transport of bacterial photosynthesis.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A genus of HALOBACTERIACEAE whose growth requires a high concentration of salt. Binary fission is by constriction.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
A species of gram-negative, aerobic bacteria isolated from soil and water as well as clinical specimens. Occasionally it is an opportunistic pathogen.
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
The process in certain BACTERIA; FUNGI; and CYANOBACTERIA converting free atmospheric NITROGEN to biologically usable forms of nitrogen, such as AMMONIA; NITRATES; and amino compounds.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Proteins found in any species of bacterium.

Hsp60 is targeted to a cryptic mitochondrion-derived organelle ("crypton") in the microaerophilic protozoan parasite Entamoeba histolytica. (1/1071)

Entamoeba histolytica is a microaerophilic protozoan parasite in which neither mitochondria nor mitochondrion-derived organelles have been previously observed. Recently, a segment of an E. histolytica gene was identified that encoded a protein similar to the mitochondrial 60-kDa heat shock protein (Hsp60 or chaperonin 60), which refolds nuclear-encoded proteins after passage through organellar membranes. The possible function and localization of the amebic Hsp60 were explored here. Like Hsp60 of mitochondria, amebic Hsp60 RNA and protein were both strongly induced by incubating parasites at 42 degreesC. 5' and 3' rapid amplifications of cDNA ends were used to obtain the entire E. histolytica hsp60 coding region, which predicted a 536-amino-acid Hsp60. The E. histolytica hsp60 gene protected from heat shock Escherichia coli groEL mutants, demonstrating the chaperonin function of the amebic Hsp60. The E. histolytica Hsp60, which lacked characteristic carboxy-terminal Gly-Met repeats, had a 21-amino-acid amino-terminal, organelle-targeting presequence that was cleaved in vivo. This presequence was necessary to target Hsp60 to one (and occasionally two or three) short, cylindrical organelle(s). In contrast, amebic alcohol dehydrogenase 1 and ferredoxin, which are bacteria-like enzymes, were diffusely distributed throughout the cytosol. We suggest that the Hsp60-associated, mitochondrion-derived organelle identified here be named "crypton," as its structure was previously hidden and its function is still cryptic.  (+info)

Putidaredoxin-cytochrome p450cam interaction. Spin state of the heme iron modulates putidaredoxin structure. (2/1071)

During the monooxygenase reaction catalyzed by cytochrome P450cam (P450cam), a ternary complex of P450cam, reduced putidaredoxin, and d-camphor is formed as an obligatory reaction intermediate. When ligands such as CO, NO, and O2 bind to the heme iron of P450cam in the intermediate complex, the EPR spectrum of reduced putidaredoxin with a characteristic signal at 346 millitesla at 77 K changed into a spectrum having a new signal at 348 millitesla. The experiment with O2 was carried out by employing a mutant P450cam with Asp251 --> Asn or Gly where the rate of electron transfer from putidaredoxin to oxyferrous P450cam is considerably reduced. Such a ligand-induced EPR spectral change of putidaredoxin was also shown in situ in Pseudomonas putida. Mutations introduced into the neighborhood of the iron-sulfur cluster of putidaredoxin revealed that a Ser44 --> Gly mutation mimicked the ligand-induced spectral change of putidaredoxin. Arg109 and Arg112, which are in the putative putidaredoxin binding site of P450cam, were essential for the spectral changes of putidaredoxin in the complex. These results indicate that a change in the P450cam active site that is the consequence of an altered spin state is transmitted to putidaredoxin within the ternary complex and produces a conformational change of the 2Fe-2S active center.  (+info)

Crystallization and a 5 A X-ray diffraction study of Aphanothece sacrum ferredoxin. (3/1071)

A chloroplast-type ferredoxin containing two non-heme iron and two labile sulfur atoms per molecule was prepared from Aphanothece sacrum. Crystals were obtained by dialysis against 75% saturated a-monium sulfate solution, and belong to the tetragonal system with cell dimensions a = b = 92.2 A and c = 47.6 A, containing four molecules in an asymmetric unit. The electron density map at 5 A resolution was calculated by using the best phase angles determined by the single isomorphous replacement method coupled with the anomalous dispersion effect. An anomalous dispersion difference Fourier map for the native crystal clearly showed four humps corresponding to the iron atoms in an asymmetric unit. The electron densis surface.  (+info)

The superoxide dismutase activity of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774. (4/1071)

Desulfoferrodoxin (Dfx), a small iron protein containing two mononuclear iron centres (designated centre I and II), was shown to complement superoxide dismutase (SOD) deficient mutants of Escherichia coli [Pianzzola, M.J., Soubes M. & Touati, D. (1996) J. Bacteriol. 178, 6736-6742]. Furthermore, neelaredoxin, a protein from Desulfovibrio gigas containing an iron site similar to centre II of Dfx, was recently shown to have a significant SOD activity [Silva, G., Oliveira, S., Gomes, C.M., Pacheco, I., Liu, M.Y., Xavier, A.V., Teixeira, M., Le Gall, J. & Rodrigues-Pousada, C. (1999) Eur. J. Biochem. 259, 235-243]. Thus, the SOD activity of Dfx isolated from the sulphate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 was studied. The protein exhibits a SOD activity of 70 U x mg-1, which increases approximately 2.5-fold upon incubation with cyanide. Cyanide binds specifically to Dfx centre II, yielding a low-spin iron species with g-values at 2.27 (g perpendicular) and 1.96 (g parallel). Upon reaction of fully oxidized Dfx with the superoxide generating system xanthine/xanthine oxidase, Dfx centres I and II become partially reduced, suggesting that Dfx operates by a redox cycling mechanism, similar to those proposed for other SODs. Evidence for another SOD in D. desulfuricans is also presented - this enzyme is inhibited by cyanide, and N-terminal sequence data strongly indicates that it is an analogue to Cu,Zn-SODs isolated from other sources. This is the first indication that a Cu-containing protein may be present in a sulphate-reducing bacterium.  (+info)

Organization and expression of nitrogen-fixation genes in the aerobic nitrogen-fixing unicellular cyanobacterium Synechococcus sp. strain RF-1. (5/1071)

Sixteen nif and 'nif-associated' genes (expressed only under conditions of nitrogen fixation) in Synechococcus sp. strain RF-1 have been cloned and sequenced. All of the nif and nif-associated genes identified in Synechococcus RF-1 were arranged in a continuous cluster spanning approximately 18 kb and containing seven operons. The nifH operon (nifH-nifD-nifK) has been reported previously. nifB, fdxN, nifS, nifU and nifP were found to be located upstream of the nifH operon. nifB-fdxN-nifS-nifU were expressed as an operon. A nifP-like gene was found to be located just upstream of nifB. nifE, nifN, nifX, nifW and the nif-associated hesA, hesB and 'fdx' were found to be located downstream from nifK. The genes located downstream from nifK are arranged nifE-nifN-nifX-orf-nifW-hesA-hesB-'+ ++fdx' and span approximately 7 kb. The function of the ORF situated between nifX and nifW is not known. However, it was identified as a counterpart of ORF-2 in Anabaena sp. strain PCC 7120 based on the deduced amino acid sequence. Northern hybridization and primer extension analysis indicated that the nif and nif-associated genes are organized in nifE-nifN, nifX-orf, nifW-hesA-hesB and 'fdx'-containing operons, respectively. According to the results of this study and previous reports, the genes are expressed in a rhythmic pattern with peaks during the dark phase when the culture is grown in a 12 h light/12 h dark regimen. The rhythm persisted after the culture was transferred to continuous illumination.  (+info)

A novel aromatic-ring-hydroxylating dioxygenase from the diterpenoid-degrading bacterium Pseudomonas abietaniphila BKME-9. (6/1071)

Pseudomonas abietaniphila BKME-9 is able to degrade dehydroabietic acid (DhA) via ring hydroxylation by a novel dioxygenase. The ditA1, ditA2, and ditA3 genes, which encode the alpha and beta subunits of the oxygenase and the ferredoxin of the diterpenoid dioxygenase, respectively, were isolated and sequenced. The ferredoxin gene is 9. 2 kb upstream of the oxygenase genes and 872 bp upstream of a putative meta ring cleavage dioxygenase gene, ditC. A Tn5 insertion in the alpha subunit gene, ditA1, resulted in the accumulation by the mutant strain BKME-941 of the pathway intermediate, 7-oxoDhA. Disruption of the ferredoxin gene, ditA3, in wild-type BKME-9 by mutant-allele exchange resulted in a strain (BKME-91) with a phenotype identical to that of the mutant strain BKME-941. Sequence analysis of the putative ferredoxin indicated that it is likely to be a [4Fe-4S]- or [3Fe-4S]-type ferredoxin and not a [2Fe-2S]-type ferredoxin, as found in all previously described ring-hydroxylating dioxygenases. Expression in Escherichia coli of ditA1A2A3, encoding the diterpenoid dioxygenase without its putative reductase component, resulted in a functional enzyme. The diterpenoid dioxygenase attacks 7-oxoDhA, and not DhA, at C-11 and C-12, producing 7-oxo-11, 12-dihydroxy-8,13-abietadien acid, which was identified by 1H nuclear magnetic resonance, UV-visible light, and high-resolution mass spectrometry. The organization of the genes encoding the various components of the diterpenoid dioxygenase, the phylogenetic distinctiveness of both the alpha subunit and the ferredoxin component, and the unusual Fe-S cluster of the ferredoxin all suggest that this enzyme belongs to a new class of aromatic ring-hydroxylating dioxygenases.  (+info)

A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. (7/1071)

The bacterium Sphingomonas sp. strain RW1 is able to use dibenzo-p-dioxin, dibenzofuran, and several hydroxylated derivatives as sole sources of carbon and energy. We have determined and analyzed the nucleic acid sequence of a 9,997-bp HindIII fragment downstream of cistrons dxnA1A2, which encode the dioxygenase component of the initial dioxygenase system of the corresponding catabolic pathways. This fragment contains 10 colinear open reading frames (ORFs), apparently organized in one compact operon. The enzymatic activities of some proteins encoded by these genes were analyzed in the strain RW1 and, after hyperexpression, in Escherichia coli. The first three ORFs of the locus, designated dxnC, ORF2, and fdx3, specify a protein with a low homology to bacterial siderophore receptors, a polypeptide representing no significant homology to known proteins, and a putative ferredoxin, respectively. dxnD encodes a 69-kDa phenol monooxygenase-like protein with activity for the turnover of 4-hydroxysalicylate, and dxnE codes for a 37-kDa protein whose sequence and activity are similar to those of known maleylacetate reductases. The following gene, dxnF, encodes a 33-kDa intradiol dioxygenase which efficiently cleaves hydroxyquinol, yielding maleylacetate, the ketoform of 3-hydroxy-cis,cis-muconate. The heteromeric protein encoded by dxnGH is a 3-oxoadipate succinyl coenzyme A (succinyl-CoA) transferase, whereas dxnI specifies a protein exhibiting marked homology to acetyl-CoA acetyltransferases (thiolases). The last ORF of the sequenced fragment codes for a putative transposase. DxnD, DxnF, DxnE, DxnGH, and DxnI (the activities of most of them have also been detected in strain RW1) thus form a complete 4-hydroxysalicylate/hydroxyquinol degradative pathway. A route for the mineralization of the growth substrates 3-hydroxydibenzofuran and 2-hydroxydibenzo-p-dioxin in Sphingomonas sp. strain RW1 thus suggests itself.  (+info)

Inorganic Fe2+ formation upon Fe-S protein thermodestruction in the membranes of thermophilic cyanobacteria: Mossbauer spectroscopy study. (8/1071)

A model description of the Mossbauer spectrum (80 K) of native membranes of the thermophilic cyanobacterium Synechococcus elongatus is suggested on the basis of the known values of quadrupole splitting (deltaE(Q)) and isomer shift (deltaFe) for the iron-containing components of the photosynthetic apparatus. Using this approach, we found that heating the membranes at 70-80 K results in a decrease of doublet amplitudes belonging to F(X), F(A), F(B) and ferredoxin and simultaneous formation of a new doublet with deltaE(Q) = 3.10 mm/s and delta-Fe = 1.28 mm/s, typical of inorganic hydrated forms of Fe2+. The inhibition of electron transfer via photosystem I to oxygen, catalyzed by ferredoxin, occurs within the same range of temperatures. The data demonstrate that the processes of thermoinduced Fe2+ formation and distortions in the photosystem I electron transport in the membranes are interrelated and caused mainly by the degradation of ferredoxin. The possible role of Fe2+ formation in the damage of the photosynthetic apparatus resulting from heating and the action of other extreme factors is discussed.  (+info)

Some ferredoxins have a sufficiently high redox potential that they can be directly reduced by NADPH. One such ferredoxin is ... Ferredoxin-2 participates in heme A and iron-sulphur protein synthesis. The [Fe4S4] ferredoxins may be further subdivided into ... "Entrez Gene: FDX1 ferredoxin 1". "FDX2 ferredoxin 2 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 8 ... Ferredoxins can be classified according to the nature of their iron-sulfur clusters and by sequence similarity. Ferredoxins ...
... (also adrenodoxin (ADX), adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin-1 (FDX1)) is a protein that ... Coghlan VM, Vickery LE (1991). "Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and ... "Entrez Gene: FDX1 ferredoxin 1". Hanukoglu I, Jefcoate CR (Apr 1980). "Mitochondrial cytochrome P-450scc. Mechanism of electron ... Mittal S, Zhu YZ, Vickery LE (Sep 1988). "Molecular cloning and sequence analysis of human placental ferredoxin". Arch Biochem ...
... may refer to: Ferredoxin-NADP(+) reductase (FNR) Ferredoxin-NAD(+) reductase Ferredoxin-nitrite reductase ... Ferredoxin-thioredoxin reductase This set index page lists enzyme articles associated with the same name. If an internal link ...
The systematic name of this enzyme is hydrogen:ferredoxin oxidoreductase Ferredoxin hydrogenase belongs to the family of ... Ferredoxin hydrogenase catalyzes the following reversible reaction: H2 + 2 oxidized ferredoxin ⇌ {\displaystyle \ ... The two substrates of this enzyme are H2 and oxidized ferredoxin, whereas its two products are reduced ferredoxin and H+. ... Ferredoxin hydrogenase has an active metallocluster site referred to as an "H-cluster" or "H domain" that is involved in the ...
Structurally, the ferredoxin fold can be regarded as a long, symmetric hairpin that is wrapped once around, so that its two ... In protein structure, a ferredoxin fold is a common α+β protein fold with a signature βαββαβ secondary structure along its ... SCOP list of proteins with a ferredoxin-like fold v t e (Protein folds, All stub articles, Protein stubs). ...
... reduced ferredoxin Thus, the two substrates of this enzyme are (3Z)-phytochromobilin and oxidized ferredoxin, whereas its two ... The systematic name of this enzyme class is (3Z)-phytochromobilin:ferredoxin oxidoreductase. Other names in common use include ... In enzymology, a phytochromobilin:ferredoxin oxidoreductase (EC 1.3.7.4) is an enzyme that catalyzes the chemical reaction (3Z ... Frankenberg N, Mukougawa K, Kohchi T, Lagarias JC (2001). "Functional genomic analysis of the HY2 family of ferredoxin- ...
... reduced ferredoxin Thus, the two substrates of this enzyme are (3Z)-phycocyanobilin and oxidized ferredoxin, whereas its two ... In enzymology, a phycocyanobilin:ferredoxin oxidoreductase (PcyA, EC 1.3.7.5) is an enzyme that catalyzes the chemical reaction ... Frankenberg N, Mukougawa K, Kohchi T, Lagarias JC (2001). "Functional genomic analysis of the HY2 family of ferredoxin- ... The systematic name of this enzyme class is (3Z)-phycocyanobilin:ferredoxin oxidoreductase. This enzyme participates in ...
In photosynthesizing tissues, it uses ferredoxin that is reduced by PSI and in the root it uses a form of ferredoxin (FdIII) ... 6 reduced ferredoxin + 7 H+ The 3 substrates of this enzyme are NH3, H2O, and oxidized ferredoxin, whereas its 3 products are ... In enzymology, a ferredoxin-nitrite reductase (EC 1.7.7.1) is an enzyme that catalyzes the chemical reaction NH3 + 2 H2O + 6 ... Hanke, G. T.; Kimata-Ariga, Y.; Taniguchi, I.; Hase, T. (2004). "A Post Genomic Characterization of Arabidopsis Ferredoxins". ...
Other names in common use include assimilatory nitrate reductase, nitrate (ferredoxin) reductase, and assimilatory ferredoxin- ... 2 reduced ferredoxin + 2 H+ The 3 substrates of this enzyme are nitrite, H2O, and oxidized ferredoxin, whereas its 3 products ... In enzymology, a ferredoxin-nitrate reductase (EC 1.7.7.2) is an enzyme that catalyzes the chemical reaction nitrite + H2O + 2 ... doi:10.1016/S0981-9428(99)80070-9. Mikami B, Ida S (December 1984). "Purification and properties of ferredoxin-nitrate ...
... and oxidized ferredoxin, whereas its 3 products are S-2-(indol-3-yl)acetyl-CoA, CO2, and reduced ferredoxin. This enzyme ... oxidized ferredoxin ⇌ {\displaystyle \rightleftharpoons } S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin The 3 ... ferredoxin), and IOR. Mai X, Adams MW (1994). "Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon ... In enzymology, an indolepyruvate ferredoxin oxidoreductase (EC 1.2.7.8) is an enzyme that catalyzes the chemical reaction ( ...
... reductase ferredoxin reductase NAD+-ferredoxin reductase ferredoxin-NAD+ reductase ferredoxin-linked NAD+ reductase ferredoxin- ... NADH-ferredoxin oxidoreductase reduced nicotinamide adenine dinucleotide-ferredoxin NADH-ferredoxin reductase NADH flavodoxin ... In enzymology, a ferredoxin-NAD+ reductase (EC 1.18.1.3) is an enzyme that catalyzes the chemical reaction: reduced ferredoxin ... The systematic name of this enzyme is ferredoxin:NAD+ oxidoreductase. There are a variety of names in common use: ferredoxin- ...
... reduced ferredoxin Thus, the two substrates of this enzyme are (3Z)-phycoerythrobilin and oxidized ferredoxin, whereas its two ... The systematic name of this enzyme class is (3Z)-phycoerythrobilin:ferredoxin oxidoreductase. This enzyme is also called PebB. ... In enzymology, a phycoerythrobilin:ferredoxin oxidoreductase (EC 1.3.7.3) is an enzyme that catalyzes the chemical reaction (3Z ... Frankenberg N, Mukougawa K, Kohchi T, Lagarias JC (2001). "Functional genomic analysis of the HY2 family of ferredoxin- ...
... ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized), reductase ferredoxin-TPN reductase, NADP+:ferredoxin ... Ferredoxin: NADP+ reductase then transfers an electron from each of two ferredoxin molecules to a single molecule of the two ... Seeber F, Aliverti A, Zanetti G (2005). "The plant-type ferredoxin-NADP+ reductase/ferredoxin redox system as a possible drug ... February 2001). "Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase". Nature ...
2 reduced ferredoxin + 2 H+ Thus, the two substrates of this enzyme are 5-methyltetrahydrofolate and oxidized ferredoxin, ... The systematic name of this enzyme class is 5-methyltetrahydrofolate:ferredoxin oxidoreductase. This enzyme is also called 5,10 ... In enzymology, a methylenetetrahydrofolate reductase (ferredoxin) (EC 1.5.7.1) is an enzyme that catalyzes the chemical ... whereas its 3 products are 5,10-methylenetetrahydrofolate, reduced ferredoxin, and H+. This enzyme belongs to the family of ...
... (EC 1.8.7.1, ferredoxin-sulfite reductase) is an enzyme with systematic name hydrogen-sulfide: ... ferredoxin oxidoreductase. This enzyme catalises the following chemical reaction hydrogen sulfide + 6 oxidized ferredoxin + 3 ... Sulfite+reductase+(ferredoxin) at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.8.7 ... H2O ⇌ {\displaystyle \rightleftharpoons } sulfite + 6 reduced ferredoxin + 6 H+ This sulfite reductase is an iron protein. ...
... EC 1.8.7.2, systematic name ferredoxin:thioredoxin disulfide oxidoreductase, is a [4Fe-4S] ... This proceeds with the attraction between FTR Lys-47 and Ferredoxin Glu-92. One electron from Ferredoxin and one electron from ... In the light, photosynthesis harnesses light energy and reduces Ferredoxin. Using FTR, reduced Ferredoxin then reduces ... plants use Ferredoxin-thioredoxin reductase for carbon fixation regulation. FTR, as part of a greater Ferredoxin-Thioredoxin ...
... ferredoxin-dependent glutamate synthase, ferredoxin-glutamate synthase, glutamate synthase (ferredoxin-dependent), and ... 2 reduced ferredoxin + 2 H+ Thus, the two substrates of this enzyme are L-glutamate and oxidized ferredoxin, whereas its 4 ... In enzymology, a glutamate synthase (ferredoxin) (EC 1.4.7.1) is an enzyme that catalyzes the chemical reaction 2 L-glutamate ... The systematic name of this enzyme class is L-glutamate:ferredoxin oxidoreductase (transaminating). Other names in common use ...
... is a member of an AOR family, which includes glyceraldehyde-3-phosphate ferredoxin ... This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase ( ... 2 oxidized ferredoxin ⇌ an acid + 2 H+ + 2 reduced ferredoxin This enzyme belongs to the family of oxidoreductases, ... With formaldehyde ferredoxin oxidoreductase, Glu308 and Tyr 416 would be involved while Glu313 and His448 is shown to be ...
... ferredoxin oxidoreductase. This enzyme catalyses the following chemical reaction 2 H2 + NAD+ + 2 oxidized ferredoxin ⇌ {\ ... Hydrogenase+(NAD+,+ferredoxin) at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (EC ... Hydrogenase (NAD+, ferredoxin) (EC 1.12.1.4, bifurcating [FeFe] hydrogenase) is an enzyme with systematic name hydrogen:NAD+, ... Schut GJ, Adams MW (July 2009). "The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a ...
... reduced ferredoxin The 3 substrates of this enzyme are CO, H2O, and oxidized ferredoxin, whereas its two products are CO2 and ... In enzymology, a carbon-monoxide dehydrogenase (ferredoxin) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction CO ... The systematic name of this enzyme class is carbon-monoxide,water:ferredoxin oxidoreductase. Meyer O, Schlegel HG (1980). " ... reduced ferredoxin. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo ...
... and oxidized ferredoxin, whereas its 3 products are 3-phospho-D-glycerate, H+, and reduced ferredoxin. This enzyme belongs to ... 2 oxidized ferredoxin ⇌ {\displaystyle \rightleftharpoons } 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin The 3 ... and glyceraldehyde-3-phosphate ferredoxin reductase. Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin ... The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use ...
... reduced ferredoxin The two substrates of this enzyme are 15,16-dihydrobiliverdin and oxidized ferredoxin, whereas its two ... 15,16-dihydrobiliverdin:ferredoxin oxidoreductase (EC 1.3.7.2) is an enzyme that catalyzes the following chemical reaction 15, ... 15,16-dihydrobiliverdin:ferredoxin oxidoreductase belongs to the family of oxidoreductases, specifically those acting on the CH ... The systematic name of this enzyme class is 15,16-dihydrobiliverdin:ferredoxin oxidoreductase. This enzyme is also called PebA ...
... ferredoxin), VOR, branched-chain ketoacid ferredoxin reductase, branched-chain oxo acid ferredoxin reductase, keto-valine- ... ferredoxin oxidoreductase, ketoisovalerate ferredoxin reductase, and 2-oxoisovalerate ferredoxin reductase. Heider J, Mai X, ... reduced ferredoxin The 3 substrates of this enzyme are 3-methyl-2-oxobutanoate, CoA, and oxidized ferredoxin, whereas its 3 ... In enzymology, a 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) (EC 1.2.7.7) is an enzyme that catalyzes the chemical ...
... ferredoxin. It is probable that Natronomonas uses ferredoxin and not NADH as the electron donor for all three reductive ... This is evident from the occurrence of conserved ferredoxin-binding residues within the N. pharaonis NirA protein and ... ferredoxin dependence of nitrate and nitrite reductases in the halophile Haloferax mediterranei. Strains of N. pharaonis were ...
The electrons are transported over ferredoxins. Fe-Fe-hydrogenases (enzymes) combine them into hydrogen gas. In Chlamydomonas ... "Identification of Global Ferredoxin Interaction Networks in Chlamydomonas reinhardtii". Journal of Biological Chemistry. 288 ( ...
... reduced ferredoxin The 3 substrates of this enzyme are pyruvate, CoA, and oxidized ferredoxin, whereas its 3 products are ... ferredoxin oxidoreductase, pyruvic-ferredoxin oxidoreductase. PFOR adopts a dimeric structure, while each monomeric subunit is ... Evans MC, Buchanan BB (1965). "Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from ... The systematic name of this enzyme class is pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating). Other names in common use ...
PMR characterization of alfalfa and soybean ferredoxins: the existence of two ferredoxins in soybean. Biochemical and ... His particular interests were ferredoxins, and lysozyme. He also had a strong interest in the NMR and ESR of nucleic acids and ... McDonald, C. C.; Phillips, W. D.; Lovenberg, W.; Holm, R. H. PMR studies on Clostridium pasteurianum ferredoxin. Origins of ... Proton magnetic resonance studies of the ferredoxins from spinach and parsley. Proceedings of the National Academy of Sciences ...
In photosynthesizing tissues, it uses an isoform of ferredoxin (Fd1) that is reduced by PSI while in the root it uses a form of ... Nitrite is then reduced to ammonia in the chloroplasts (plastids in roots) by a ferredoxin dependent nitrite reductase. ... Hanke, G. T.; Kimata-Ariga, Y.; Taniguchi, I.; Hase, T. (2004). "A Post Genomic Characterization of Arabidopsis Ferredoxins". ... ferredoxin (Fd3) that has a less negative midpoint potential and can be reduced easily by NADPH. In non photosynthesizing ...
Ferredoxin 2 is a protein that in humans is encoded by the FDX2 gene. It participates in heme A synthesis and iron-sulphur ... "Entrez Gene: Ferredoxin 2". Spiegel R, Saada A, Halvardson J, Soiferman D, Shaag A, Edvardson S, Horovitz Y, Khayat M, Shalev ... "Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster ...
It employs one cofactor, ferredoxin. The 3 substrates of this enzyme are stearoyl-(acyl-carrier-protein), reduced acceptor, and ... the fatty acid composition of Escherichia coli by coexpression of a plant acyl-acyl carrier protein desaturase and ferredoxin ... Carrier Protein and Unusual Acyl-Acyl Carrier Protein Desaturase Activities Are Differentially Influenced by Ferredoxin". Plant ...
The amino acid sequence of Clostridium pasteurianum ferredoxin. scientific article published on 01 May 1966 ...
NADP+ reductase for site-specific ferredoxin mutants. Biochemistry (1997) Release Date. 2001-05-23. Peptides. FERREDOXIN I: A. ... STRUCTURE OF THE ANABAENA FERREDOXIN MUTANT E95K Coordinates. PDB Format Method. X-RAY DIFFRACTION 1.80 Å. Oligo State. monomer ... Hurley, J.K. et al., Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, ... reduction potentials, and rate constants of electron transfer to ferredoxin: ...
BRENDA - The Comprehensive Enzyme Information System
Structure of the bacterial plant-ferredoxin receptor FusA. Home/Publications/Structure of the bacterial plant-ferredoxin ... to obtain iron from plant ferredoxin. Through the crystal structure of FusA we show that binding of ferredoxin occurs through ... Structure of the bacterial plant-ferredoxin receptor FusA. (2016). Nature Communications. Published online 31 October 2016. doi ... specialized extracellular loops that form extensive interactions with ferredoxin. The function of FusA and the presence of ...
Dive into the research topics of Molecular dynamics simulations of Trichomonas vaginalis ferredoxin show a loop-cap transition ... Molecular dynamics simulations of Trichomonas vaginalis ferredoxin show a loop-cap transition. ...
Differential activities of heterocyst ferredoxin, vegetative cell ferredoxin, and flavodoxin as electron carriers in nitrogen ... Setif, P. Ferredoxin and flavodoxin reduction by photosystem I. Biochim. Biophys. Acta 2001, 1507, 161-179. [Google Scholar] ... Giro, M.; Carrillo, N.; Krapp, A.R. Glucose-6-phosphate dehydrogenase and ferredoxin-NADP(H) reductase contribute to damage ... either a ferredoxin (Fd) or a Fld [5]. Rhodobacter capsulatus is a non-sulphur purple bacterium capable of fixating atmospheric ...
We further demonstrated that cKMT1 could methylate ferredoxin-NADP(+) oxidoreductase (FNR) and its potential sites of action on ... cKMT1 is a New Lysine Methyltransferase That Methylates the Ferredoxin-NADP(+) Oxidoreductase and Regulates Energy Transfer in ...
ADE2 Overexpression Lysate. Tested Reactivity: Hu. Validated: WB. Backed by our 100% Guarantee.
FE - Ferredoxin. FE - Free Energy. Fe - Iron. FGC - Flue Gas Conditioning. FIGD - Flow Injection/Gas Diffusion. FIGE - Field ...
4Fe-4S ferredoxins View. Download. 0.204. 0.688. 3-5-exoribonuclease activity. f.13.1. Family A G protein-coupled receptor- ...
Superfamily d.15.4: 2Fe-2S ferredoxin-like [54292] (3 families) *. Family d.15.4.2: 2Fe-2S ferredoxin domains from multidomain ...
a), Table S1]. The overall structure reveals a ferredoxin-like fold typical of dye decolourizing peroxidases (Sugano, 2009. ) ...
UniProt: 4Fe-4S ferredoxin-type 2. 389 -> 411 PVGCIELGEVKFKKGEKEHPVTL UniProt: In Ref. 3; M59444.. ...
It elicits antiprotozoal activity by interfering with pyruvate-ferredoxin oxidoreductase (PFOR) enzyme-dependent electron ...
The dimer of FeS(SCH3)2- is a simple model for ferredoxins, a class of proteins that facilitate electron transfer reactions in ...
sn-2 acyl-lipid omega-3 desaturase (ferredoxin). 1.14.19.36. sn-1 acyl-lipid omega-3 desaturase (ferredoxin). ...
Ferredoxin. Ferredoxin I. Ferredoxin II. Ferredoxin III. Tree number(s):. D12.776.097.350. D12.776.157.427.374.375.275. D12.776 ... Ferredoxins - Preferred Concept UI. M0008347. Scope note. Iron-containing proteins that transfer electrons, usually at a low ...
Analysis of a rdxA gene and involvement of additional genes encoding NADPH flavin oxidoreductase (FrxA) and ferredoxin-like ...
1CZP: Anabaena Pcc7119 [2fe-2s] Ferredoxin In The Reduced And Oxix At 1.17 A reference: Refined X-ray structures of the ... oxidized, at 1.3 A, and reduced, at 1.17 A, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked ...
Recommended name: reduced_ferredoxin_[iron-sulfur]_cluster Link to BRENDA ligand page. ...
A four iron ferredoxin from Desulfovibrio desulfuricans. Zubieta, J. A., Mason, R. & Postgate, J. R., 1973, In: Biochemical ...
... including replacement of the iron-requiring ferredoxin electron shuttle protein with a less-efficient iron-free flavodoxin ...
... from the chlorophyll molecule in the reaction center of photosystem I is transferred to a molecule called ferredoxin. From ...
KOR, 2-oxoglutarate/2-oxoacid ferredoxin oxidoreductase; BUK, butyrate kinase; ENO, enolase; ENR, enoyl-[acyl-carrier protein] ... ferredoxin oxidoreductase; ACS, acetyl-CoA synthase; ACK, acetate kinase; ACAT, acetyl-CoA acetyltransferase; BCoAT, butyryl ...
Description: A Monoclonal antibody against Human Ferredoxin Reductase (Clone 6C2). The antibodies are raised in Mouse and are ...
Ferredoxin-Thioredoxin Reductase - Properties of its Complex with Ferredoxin .3.. Ferredoxin-Thioredoxin Reductase - Properties ... of its Complex with Ferredoxin .3.. by Hirasawa, Masakazu; Droux, M.; Gray, Kevin A.; Boyer, J. Milton; Davis, Dan J.; Buchanan ...
2-oxoglutarate ferredoxin oxidoreductase subunit beta (RefSeq). 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; Short= ... pyruvate ferredoxin/flavodoxin oxidoreductase, beta subunit (RefSeq). 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; ... 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; Short=OFOR1; EC 1.2.7.11 (characterized, see rationale). 33%. 62%. 95.5. ... 3 candidates for ofob: 2-oxobutanoate:ferredoxin oxidoreductase, beta subunit. Score. Gene. Description. Similar to. Id.. Cov. ...
  • Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants. (expasy.org)
  • However, while Fd2 can efficiently react with photosystem I or nitrite reductase, time-resolved spectroscopy shows that Fd2 has a very low capacity to reduce ferredoxin-NADP + oxidoreductase (FNR). (elsevierpure.com)
  • Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. (nih.gov)
  • Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. (nih.gov)
  • Pyruvate ferredoxin oxidoreductase (PFOR) is central to the anaerobic metabolism of many bacteria and amitochondriate eukaryotes. (nebraska.edu)
  • cKMT1 is a New Lysine Methyltransferase That Methylates the Ferredoxin-NADP(+) Oxidoreductase and Regulates Energy Transfer in Cyanobacteria. (bvsalud.org)
  • We further demonstrated that cKMT1 could methylate ferredoxin - NADP (+) oxidoreductase (FNR) and its potential sites of action on FNR were identified. (bvsalud.org)
  • It elicits antiprotozoal activity by interfering with pyruvate-ferredoxin oxidoreductase (PFOR) enzyme-dependent electron transfer reaction, which is essential to anaerobic energy metabolism. (medscape.com)
  • Photosynthetic [2Fe-2S] plant-type ferredoxins have a central role in electron transfer between the photosynthetic chain and various metabolic pathways. (elsevierpure.com)
  • 7. Complete amino acid sequence of ferredoxin from Peridinium bipes (Dinophyceae). (nih.gov)
  • 14. Amino acid sequence of Chlorogloeopsis fritschii ferredoxin: taxonomic and evolutionary aspects. (nih.gov)
  • 15. Amino acid sequence of a ferredoxin from Bumilleriopsis filiformis, a yellow-green alga: relationship with red algae, protoflorideophyceae, and filamentous blue-green algae. (nih.gov)
  • 17. Amino acid sequence of Synechocystis 6714 ferredoxin: a unique structural feature of unicellular blue-green algal ferredoxin. (nih.gov)
  • PFOR contains thiamine pyrophosphate (TPP) and three [4Fe-4S] clusters, which link pyruvate oxidation to reduction of ferredoxin. (nebraska.edu)
  • We report the structural and functional properties of a novel minor type ferredoxin, Fd2 of T. elongatus, homologous to Fed4 from Synechocystis sp. (elsevierpure.com)
  • Several genes are coding for [2Fe-2S] ferredoxins in cyanobacteria, with four in the thermophilic cyanobacterium Thermosynechococcus elongatus. (elsevierpure.com)
  • This gene encodes a member of the ferredoxin family. (nih.gov)
  • This gene encodes a protein which contains a ferredoxin-fold anticodon-binding domain which is contained in a subset of phenylalanyl tRNA synthetases. (nih.gov)
  • The encoded protein contains a 2Fe-2S ferredoxin-type domain and is essential for heme A and Fe/S protein biosynthesis. (nih.gov)
  • Through the crystal structure of FusA we show that binding of ferredoxin occurs through specialized extracellular loops that form extensive interactions with ferredoxin. (bioexcel.eu)
  • The structure and functional properties of the major ferredoxin Fd1 are well known but data on the other ferredoxins are scarce. (elsevierpure.com)
  • The Fd2 structure significantly differs from other known ferredoxins structures in loop 2, N-terminal region, hydrogen bonding networks and surface charge distributions. (elsevierpure.com)