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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/04/01 07:24:31」(JST)

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Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron-sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.^[1]^[2]

Another redox protein, isolated from spinach chloroplasts by Tagawa and Arnon in 1962, was termed "chloroplast ferredoxin".^[3] The chloroplast ferredoxin is involved in both cyclic and non-cyclic photophosphorylation reactions of photosynthesis. In non-cyclic photophosphorylation, ferredoxin is the last electron acceptor and reduces the enzyme NADP⁺ reductase. It accepts electrons produced from sunlight-excited chlorophyll and transfers them to the enzyme ferredoxin:NADP⁺ oxidoreductase EC 1.18.1.2.

Ferredoxins are small proteins containing iron and sulfur atoms organized as iron-sulfur clusters. These biological "capacitors" can accept or discharge electrons, the effect being change in the oxidation states (+2 or +3) of the iron atoms. This way, ferredoxin acts as electron transfer agents in biological redox reactions.

Other bioinorganic electron transport systems include rubredoxins, cytochromes, blue copper proteins, and the structurally related Rieske proteins.

Ferredoxins can be classified according to the nature of their iron-sulfur clusters and by sequence similarity.

1 Fe₂S₂ ferredoxins
- 1.1 Plant-type ferredoxins
- 1.2 Thioredoxin-like ferredoxins
- 1.3 Adrenodoxin-type ferredoxins
2 Fe₄S₄ and Fe₃S₄ ferredoxins
- 2.1 Bacterial-type ferredoxins
- 2.2 High-potential iron-sulfur proteins
3 Human proteins from ferredoxin family
4 References
5 Further reading
6 External links

Fe₂S₂ ferredoxins[edit]

Members of the 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2), which includes putidaredoxin and terpredoxin, and adrenodoxin.^[4]^[5]^[6]^[7] They are proteins of around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This conserved region is also found as a domain in various metabolic enzymes and in multidomain proteins, such as aldehyde oxidoreductase (N-terminal), xanthine oxidase (N-terminal), phthalate dioxygenase reductase (C-terminal), succinate dehydrogenase iron-sulphur protein (N-terminal), and methane monooxygenase reductase (N-terminal).

Plant-type ferredoxins[edit]

One group of ferredoxins, originally found in chloroplast membranes, has been termed "chloroplast-type" or "plant-type". The active center is a [Fe₂S₂] cluster, where the iron atoms are tetrahedrally coordinated both by inorganic sulfur atoms and by sulfurs provided by four conserved cysteine (Cys) residues.

In chloroplasts, Fe₂S₂ ferredoxins function as electron carriers in the photosynthetic electron transport chain and as electron donors to various cellular proteins, such as glutamate synthase, nitrate reductase and sulfite reductase. In hydroxylating bacterial dioxygenase systems, they serve as intermediate electron-transfer carriers between reductase flavoproteins and oxygenase.

Thioredoxin-like ferredoxins[edit]

The Fe₂S₂ ferredoxin from Clostridium pasteurianum (Cp2FeFd) has been recognized as distinct protein family on the basis of its amino acid sequence, spectroscopic properties of its iron-sulfur cluster and the unique ligand swapping ability of two cysteine ligands to the [Fe₂S₂] cluster. Although the physiological role of this ferredoxin remains unclear, a strong and specific interaction of Cp2FeFd with the molybdenum-iron protein of nitrogenase has been revealed. Homologous ferredoxins from Azotobacter vinelandii (Av2FeFdI) and Aquifex aeolicus (AaFd) have been characterized. The crystal structure of AaFd has been solved. AaFd exists as a dimer. The structure of AaFd monomer is different from other Fe₂S₂ ferredoxins. The fold belongs to the α+β class, with first four β-strands and two α-helices adopting a variant of the thioredoxin fold.

Adrenodoxin-type ferredoxins[edit]

Adrenodoxin (adrenal ferredoxin) is expressed in mammals including humans. The human variant of adrenodoxin is referred to as ferredoxin 1. Adrenodoxin, putidaredoxin, and terpredoxin are soluble Fe₂S₂ proteins that act as single electron carriers. In mitochondrial monooxygenase systems, adrenodoxin transfers an electron from NADPH:adrenodoxin reductase to membrane-bound cytochrome P450. In bacteria, putidaredoxin and terpredoxin serve as electron carriers between corresponding NADH-dependent ferredoxin reductases and soluble P450s. The exact functions of other members of this family are not known, although Escherichia coli Fdx is shown to be involved in biogenesis of Fe-S clusters. Despite low sequence similarity between adrenodoxin-type and plant-type ferredoxins, the two classes have a similar folding topology.

Ferredoxin-1 in humans participates in the synthesis of thyroid hormones. It also transfers electrons from adrenodoxin reductase to the cholesterol side chain cleavage cytochrome P450. FDX-1 has the capability to bind to metals and proteins. It can be found within the cellular mitochondrial matrix.

Fe₄S₄ and Fe₃S₄ ferredoxins[edit]

The [Fe₄S₄] ferredoxins may be further subdivided into low-potential (bacterial-type) and high-potential (HiPIP) ferredoxins.

Low- and high-potential ferredoxins are related by the following redox scheme:

The formal oxidation numbers of the iron ions can be [2Fe³⁺, 2Fe²⁺] or [1Fe³⁺, 3Fe²⁺] in low-potential ferredoxins. The oxidation numbers of the iron ions in high-potential ferredoxins can be [3Fe³⁺, 1Fe²⁺] or [2Fe³⁺, 2Fe²⁺].

Bacterial-type ferredoxins[edit]

4Fe-4S binding domain

Structural representation of an Fe₃S₄ ferredoxin.

Identifiers

Symbol

Fer4

Pfam

PF00037

InterPro

IPR001450

PROSITE

PDOC00176

SCOP

5fd1

SUPERFAMILY

5fd1

OPM protein

1kqf

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

A group of Fe₄S₄ ferredoxins, originally found in bacteria, has been termed "bacterial-type". Bacterial-type ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including four cysteine residues that bind to a [Fe₄S₄] cluster. In Pyrococcus furiosus Fe₄S₄ ferredoxin, one of the conserved Cys residues is substituted with aspartic acid.

During the evolution of bacterial-type ferredoxins, intrasequence gene duplication, transposition and fusion events occurred, resulting in the appearance of proteins with multiple iron-sulfur centers. In some bacterial ferredoxins, one of the duplicated domains has lost one or more of the four conserved Cys residues. These domains have either lost their iron-sulfur binding property or bind to a [Fe₃S₄] cluster instead of a [Fe₄S₄] cluster^[9] and dicluster-type.^[10]

3-D structures are known for a number of monocluster and dicluster bacterial-type ferredoxins. The fold belongs to the α+β class, with 2-7 α-helices and four β-strands forming a barrel-like structure, and an extruded loop containing three "proximal" Cys ligands of the iron-sulfur cluster.

High-potential iron-sulfur proteins[edit]

High-potential iron-sulfur proteins (HiPIPs) form a unique family of Fe₄S₄ ferredoxins that function in anaerobic electron transport chains. Some HiPIPs have a redox potential higher than any other known iron-sulfur protein (e.g., HiPIP from Rhodopila globiformis has a redox potential of ca. 450 mV). Several HiPIPs have so far been characterized structurally, their folds belonging to the α+β class. As in other bacterial ferredoxins, the [Fe₄S₄] cluster adopts a cubane-like conformation and is ligated to the protein via four Cys residues.

Human proteins from ferredoxin family[edit]

2Fe-2S: AOX1; FDX1; FDX1L; NDUFS1; SDHB; XDH;
4Fe-4S: ABCE1; DPYD; NDUFS8;

References[edit]

^ Mortenson LE, Valentine RC, Carnahan JE (June 1962). "An electron transport factor from Clostridium pasteurianum". Biochem. Biophys. Res. Commun. 7: 448–52. doi:10.1016/0006-291X(62)90333-9. PMID 14476372.
^ Valentine RC (December 1964). "Bacterial ferredoxin". Bacteriol Rev 28: 497–517. PMC 441251. PMID 14244728.
^ Tagawa K, Arnon DI (August 1962). "Ferredoxins as electron carriers in photosynthesis and in the biological production and consumption of hydrogen gas". Nature 195 (4841): 537–43. Bibcode:1962Natur.195..537T. doi:10.1038/195537a0. PMID 14039612.
^ Jouanneau Y, Armengaud J, Sainz G, Sieker LC (2001). "Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus". Acta Crystallogr. D 57 (Pt 2): 301–303. doi:10.1107/S0907444900017832. PMID 11173487.
^ Sevrioukova IF (2005). "Redox-dependent Structural Reorganization in Putidaredoxin, a Vertebrate-type [2Fe-2S] Ferredoxin from Pseudomonas putida". J. Mol. Biol. 347 (3): 607–621. doi:10.1016/j.jmb.2005.01.047. PMID 15755454.
^ Pochapsky TC, Mo H, Pochapsky SS (1999). "A model for the solution structure of oxidized terpredoxin, a Fe2S2 ferredoxin from Pseudomonas". Biochemistry 38 (17): 5666–5675. doi:10.1021/bi983063r. PMID 10220356.
^ Ruterjans H, Beilke D, Weiss R, Lohr F, Pristovsek P, Hannemann F, Bernhardt R (2002). "A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin". Biochemistry 41 (25): 7969–7978. doi:10.1021/bi0160361. PMID 12069587.
^ PDB 3P1M; Chaikuad A, Johansson, C, Krojer, T, Yue, WW, Phillips, C, Bray, JE, Pike, ACW, Muniz, JRC, Vollmar, M, Weigelt, J, Arrowsmith, CH, Edwards, AM, Bountra, C, Kavanagh, K, Oppermann, U (2010). "Crystal structure of human ferredoxin-1 (FDX1) in complex with iron-sulfur cluster". To be published. doi:10.2210/pdb3p1m/pdb.
^ Fukuyama K, Matsubara H, Katsube Y, Tsukihara T (1989). "Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 A resolution. Structural comparisons of bacterial ferredoxins". J. Mol. Biol. 210 (2): 383–398. doi:10.1016/0022-2836(89)90338-0. PMID 2600971.
^ Sieker LC, Meyer J, Moulis JM, Fanchon E, Duee ED, Vicat J (1994). "Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 A resolution". J. Mol. Biol. 243 (4): 683–695. doi:10.1016/0022-2836(94)90041-8. PMID 7966291.

External links[edit]

IPR006057 - 2Fe-2S ferredoxin subdomain
IPR001055 - Adrenodoxin
IPR001450 - 4Fe-4S ferredoxin, iron-sulfur binding
IPR000170 - High potential iron-sulfur protein
PDB 1F37 - X-ray structure of thioredoxin-like ferredoxin from Aquifex aeolicus (AaFd)

UpToDate Contents

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1. メトロニダゾール：概要 metronidazole an overview
2. 脳腱黄色腫症 cerebrotendinous xanthomatosis

English Journal

Role of transcription and enzyme activities in redistribution of carbon and electron flux in response to N2 and H 2 sparging of open-batch cultures of Clostridium thermocellum ATCC 27405.

Carere CR1, Rydzak T, Cicek N, Levin DB, Sparling R.Author information 1Department of Biosystems Engineering, University of Manitoba, Winnipeg, MB, Canada, R3T 5V6, umcarerc@cc.umanitoba.ca.AbstractGrowth, end-product synthesis, enzyme activities, and transcription of select genes associated with the "malate shunt," pyruvate catabolism, H2 synthesis, and ethanol production were studied in the cellulolytic anaerobe, Clostridium thermocellum ATCC 27405, during open-batch fermentation of cellobiose to determine the effect of elevated N2 and H2 gas sparging on metabolism using a 14-L fermenter with a 7-L working volume. The metabolic shift from acetate, H2, and CO2 to ethanol and formate in response to high H2 versus high N2 sparging (20 mL s(-1)) was accompanied by (a) a 2-fold increase in nicotinamide adenine dinucleotide (NADH)-dependent alcohol dehydrogenase (Adh) activity, (b) a 10-fold increase in adhE transcription, and (c) a 3-fold decrease in adhZ transcription. A similar, but less pronounced, metabolic shift was also observed when the rate of N2 sparging was decreased from 20 to 2 mL s(-1), during which (a) NADH-dependent ADH and pyruvate: ferredoxin oxidoreductase (PFOR) activities increased by ∼1.5-fold, (b) adhY transcription increased 6-fold, and (c) transcription of selected pfor genes increased 2-fold. Here we demonstrate that transcription of genes involved in ethanol metabolism is tightly regulated in response to gas sparging. We discuss the potential impacts of dissolved H2 on electron carrier (NADH, NADPH, ferredoxin) oxidation and how these electron carriers can redirect carbon and electron flux and regulate adhE transcription.
Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2014 Mar;98(6):2829-40. doi: 10.1007/s00253-013-5500-y. Epub 2014 Jan 25.
Growth, end-product synthesis, enzyme activities, and transcription of select genes associated with the "malate shunt," pyruvate catabolism, H2 synthesis, and ethanol production were studied in the cellulolytic anaerobe, Clostridium thermocellum ATCC 27405, during open-batch fermentation of cellobio
PMID 24463715

Mitochondrial and Nucleolar Localization of Cysteine Desulfurase Nfs and the Scaffold Protein Isu in Trypanosoma brucei.

Kovárová J1, Horáková E, Changmai P, Vancová M, Luke X0161 J.Author information 1Biology Center, Institute of Parasitology, Czech Academy of Sciences and Faculty of Sciences, University of South Bohemia, České Budějovice (Budweis), Czech Republic.AbstractTrypanosoma brucei has a complex life cycle during which its single mitochondrion is subjected to major metabolic and morphological changes. While the procyclic stage (PS) of the insect vector contains a large and reticulated mitochondrion, its counterpart in the bloodstream stage (BS) parasitizing mammals is highly reduced and seems to be devoid of most functions. We show here that key Fe-S cluster assembly proteins are still present and active in this organelle and that produced clusters are incorporated into overexpressed enzymes. Importantly, the cysteine desulfurase Nfs, equipped with the nuclear localization signal, was detected in the nucleolus of both T. brucei life stages. The scaffold protein Isu, an interacting partner of Nfs, was also found to have a dual localization in the mitochondrion and the nucleolus, while frataxin and both ferredoxins are confined to the mitochondrion. Moreover, upon depletion of Isu, cytosolic tRNA thiolation dropped in the PS but not BS parasites.
Eukaryotic cell.Eukaryot Cell.2014 Mar;13(3):353-362. Epub 2013 Nov 15.
Trypanosoma brucei has a complex life cycle during which its single mitochondrion is subjected to major metabolic and morphological changes. While the procyclic stage (PS) of the insect vector contains a large and reticulated mitochondrion, its counterpart in the bloodstream stage (BS) parasitizing
PMID 24243795

Conservation analysis of class-specific positions in cytochrome P450 monooxygenases: Functional and structural relevance.

Gricman L1, Vogel C, Pleiss J.Author information 1Institute of Technical Biochemistry, University of Stuttgart, 70569, Stuttgart, Germany.AbstractCytochrome P450 monooxygenases (CYPs) constitute a ubiquitous, highly divergent protein family. Nevertheless, all CYPs share a common fold and conserved catalytic machinery. Based on the electron donor system, 10 classes of CYPs have been described, but most CYPs are members of class I accepting electrons from ferredoxin which is being reduced by FAD-containing reductase, or class II accepting electrons from FAD- and FMN-containing CPR-type reductase. Because of the low sequence conservation inside the two classes, the conserved class-specific positions are expected to be involved in aspects of electron transfer that are specific to the two types of reductases. In this work we present results from a conservation analysis of 16,732 CYP sequences derived from an updated version of the Cytochrome P450 Engineering Database (CYPED), using two class-specific numbering schemes. While no position was conserved on the distal, substrate-binding surface of the CYPs, several class-specific residues were found on the proximal, reductase-interacting surface; two class I-specific residues that were negatively charged, and three class II-specific residues that were aromatic or charged. The class-specific conservation of glycine and proline residues in the cysteine pocket indicates that there are class-specific differences in the flexibility of this element. Four heme-interacting arginines were conserved differently in each class, and a class-specific substitution of a heme-interacting tyrosine by histidine was found, pointing to a link between heme stabilization and the reductase type. Proteins 2014; 82:491-504. © 2013 Wiley Periodicals, Inc.
Proteins.Proteins.2014 Mar;82(3):491-504. doi: 10.1002/prot.24415. Epub 2013 Oct 17.
Cytochrome P450 monooxygenases (CYPs) constitute a ubiquitous, highly divergent protein family. Nevertheless, all CYPs share a common fold and conserved catalytic machinery. Based on the electron donor system, 10 classes of CYPs have been described, but most CYPs are members of class I accepting ele
PMID 24105833

Japanese Journal

Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH

Seo Daisuke,Naito Hiroshi,Nishimura Erika,Sakurai Takeshi
Photosynthesis Research 125(1-2), 321-328, 2015-02-20
… Ferredoxin-NAD(P)+ oxidoreductases ([EC 1.18.1.2], [EC 1.18.1.3], FNRs) from green sulfur bacteria, purple non-sulfur bacteria and most of Firmicutes, such as Bacillus subtilis (BsFNR) are homo-dimeric flavoproteins homologous to bacterial NADPH-thioredoxin reductase. … To investigate the role of the si-face Tyr50 residue in BsFNR, we replaced Tyr50 with Gly, Ser, and Trp and examined its spectroscopic properties and enzymatic activities in the presence of NADPH and ferredoxin (Fd) from B. …
NAID 120005602822

Amino Acid Sequences of Ferredoxins from Several Species of Genus Ephedra

MINO Yoshiki,AZUMA Takashi,SATO Takaji
大阪薬科大学紀要 (9), 53-60, 2015
NAID 40020421752

Transcriptional regulation of genes related to progesterone production [Review]

Mizutani Tetsuya,Ishikane Shin,Kawabe Shinya,Umezawa Akihiro,Miyamoto Kaoru
Endocrine Journal advpub(0), 2015
… 5-Aminolevulinic acid synthase 1, ferredoxin 1, and ferredoxin reductase also play a role in steroidogenesis as accessory factors. …
NAID 130005085779

Related Pictures

★リンクテーブル★

拡張検索	「molybdoferredoxin」「NADPH-ferredoxin reductase」「ferredoxin-thioredoxin reductase」「ferredoxin-nitrite reductase」

「molybdoferredoxin」

ferredoxin 1
	; Crystal structure of human ferredoxin-1 (FDX1).
Identifiers
Symbol	FDX1
Alt. symbols	FDX
Entrez	2230
HUGO	3638
OMIM	103260
RefSeq	NM_004109
UniProt	P10109
Other data
Locus	Chr. 11 q22.3

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

2Fe-2S iron-sulfur cluster binding domain
	; Structural representation of an Fe2S2 ferredoxin.
Identifiers
Symbol	Fer2
Pfam	PF00111
InterPro	IPR001041
PROSITE	PDOC00642
SCOP	3fxc
SUPERFAMILY	3fxc
OPM protein	1kf6
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

　　[★]

モリブドフェレドキシン

関: FeMo cofactor、iron-molybdenum cofactor、MoFe protein

「NADPH-ferredoxin reductase」

　　[★]

NADPHフェレドキシン還元酵素

関: ferredoxin-NADP reductase

「ferredoxin-thioredoxin reductase」

　　[★] フェレドキシン-チオレドキシンレダクターゼ

「ferredoxin-nitrite reductase」

　　[★]

フェレドキシン亜硝酸還元酵素

[pmid14476372-1] Mortenson LE, Valentine RC, Carnahan JE (June 1962). "An electron transport factor from Clostridium pasteurianum". Biochem. Biophys. Res. Commun. 7: 448–52. doi:10.1016/0006-291X(62)90333-9. PMID 14476372.

[pmid14244728-2] Valentine RC (December 1964). "Bacterial ferredoxin". Bacteriol Rev 28: 497–517. PMC 441251. PMID 14244728.

[pmid14039612-3] Tagawa K, Arnon DI (August 1962). "Ferredoxins as electron carriers in photosynthesis and in the biological production and consumption of hydrogen gas". Nature 195 (4841): 537–43. Bibcode:1962Natur.195..537T. doi:10.1038/195537a0. PMID 14039612.

[PUB00016347-4] Jouanneau Y, Armengaud J, Sainz G, Sieker LC (2001). "Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus". Acta Crystallogr. D 57 (Pt 2): 301–303. doi:10.1107/S0907444900017832. PMID 11173487.

[PUB00016348-5] Sevrioukova IF (2005). "Redox-dependent Structural Reorganization in Putidaredoxin, a Vertebrate-type [2Fe-2S] Ferredoxin from Pseudomonas putida". J. Mol. Biol. 347 (3): 607–621. doi:10.1016/j.jmb.2005.01.047. PMID 15755454.

[PUB00016349-6] Pochapsky TC, Mo H, Pochapsky SS (1999). "A model for the solution structure of oxidized terpredoxin, a Fe2S2 ferredoxin from Pseudomonas". Biochemistry 38 (17): 5666–5675. doi:10.1021/bi983063r. PMID 10220356.

[PUB00016350-7] Ruterjans H, Beilke D, Weiss R, Lohr F, Pristovsek P, Hannemann F, Bernhardt R (2002). "A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin". Biochemistry 41 (25): 7969–7978. doi:10.1021/bi0160361. PMID 12069587.

[Chaikuad_2010-8] PDB 3P1M; Chaikuad A, Johansson, C, Krojer, T, Yue, WW, Phillips, C, Bray, JE, Pike, ACW, Muniz, JRC, Vollmar, M, Weigelt, J, Arrowsmith, CH, Edwards, AM, Bountra, C, Kavanagh, K, Oppermann, U (2010). "Crystal structure of human ferredoxin-1 (FDX1) in complex with iron-sulfur cluster". To be published. doi:10.2210/pdb3p1m/pdb.

[PUB00003253-9] Fukuyama K, Matsubara H, Katsube Y, Tsukihara T (1989). "Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 A resolution. Structural comparisons of bacterial ferredoxins". J. Mol. Biol. 210 (2): 383–398. doi:10.1016/0022-2836(89)90338-0. PMID 2600971.

[PUB00003332-10] Sieker LC, Meyer J, Moulis JM, Fanchon E, Duee ED, Vicat J (1994). "Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 A resolution". J. Mol. Biol. 243 (4): 683–695. doi:10.1016/0022-2836(94)90041-8. PMID 7966291.

匿名

検索

案内

案内

ferredoxin

Wikipedia preview

wiki en

Contents

Fe₂S₂ ferredoxins[edit]

Plant-type ferredoxins[edit]

Thioredoxin-like ferredoxins[edit]

Adrenodoxin-type ferredoxins[edit]

Fe₄S₄ and Fe₃S₄ ferredoxins[edit]

Bacterial-type ferredoxins[edit]

High-potential iron-sulfur proteins[edit]

Human proteins from ferredoxin family[edit]

References[edit]

Further reading[edit]

External links[edit]

UpToDate Contents

English Journal

Japanese Journal

Related Links

Related Pictures

★リンクテーブル★

「molybdoferredoxin」

「NADPH-ferredoxin reductase」

「ferredoxin-thioredoxin reductase」

「ferredoxin-nitrite reductase」

ferredoxin 1
Crystal structure of human ferredoxin-1 (FDX1).^[8]
Identifiers
Symbol	FDX1
Alt. symbols	FDX
Entrez	2230
HUGO	3638
OMIM	103260
RefSeq	NM_004109
UniProt	P10109
Other data
Locus	Chr. 11 q22.3

匿名

検索

案内

ferredoxin

Wikipedia preview

wiki en

Contents

Fe2S2 ferredoxins[edit]

Plant-type ferredoxins[edit]

Thioredoxin-like ferredoxins[edit]

Adrenodoxin-type ferredoxins[edit]

Fe4S4 and Fe3S4 ferredoxins[edit]

Bacterial-type ferredoxins[edit]

High-potential iron-sulfur proteins[edit]

Human proteins from ferredoxin family[edit]

References[edit]

Further reading[edit]

External links[edit]

UpToDate Contents

English Journal

Japanese Journal

Related Links

Related Pictures

★リンクテーブル★

「molybdoferredoxin」

「NADPH-ferredoxin reductase」

「ferredoxin-thioredoxin reductase」

「ferredoxin-nitrite reductase」

Fe₂S₂ ferredoxins[edit]

Fe₄S₄ and Fe₃S₄ ferredoxins[edit]