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1. 神経芽腫の治療および予後treatment and prognosis of neuroblastoma [show details]
…cells in infants with stage 4S (MS) disease have the capacity to undergo spontaneous regression . However, like all stages of neuroblastomas, the tumors that make up stage MS (4S) disease are heterogeneous …
2. メトロニダゾール：概要metronidazole an overview [show details]
…metronidazole is associated with reduced transcription activity of the ferredoxin gene that results in decreased intracellular levels of ferredoxin and reduced pyruvate:ferredoxin oxidoreductase activity. In addition…
3. 神経芽腫の疫学、病因、および病理epidemiology pathogenesis and pathology of neuroblastoma [show details]
…with stage 1, 2, or 4S disease, mean three-year event-free survival was greater among those without than with allelic loss of chromosome 1p (100 versus 34 percent for stage 1, 2, or 4S disease and 53 versus …
4. 抗凝固療法関連腎症anticoagulant related nephropathy [show details]
…required to cause ARN is not known. Most commonly, the International Normalized Ratio (INR) is in the 4s . However, factors other than the degree of coagulopathy contribute to the development of acute kidney …
5. 脳腱黄色腫症cerebrotendinous xanthomatosis [show details]
…the mitochondria and peroxisomes . Sterol 27-hydroxylase, in the presence of cofactors ferredoxin and NADPH-ferredoxin reductase, catalyzes the hydroxylation of 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol…

English Journal

Studies on the Mechanism of Electron Bifurcation Catalyzed by Electron Transferring Flavoprotein (Etf) and Butyryl-CoA Dehydrogenase (Bcd) of Acidaminococcus fermentans.

Chowdhury NP1, Mowafy AM, Demmer JK, Upadhyay V, Koelzer S, Jayamani E, Kahnt J, Hornung M, Demmer U, Ermler U, Buckel W.Author information 1From the Laboratorium für Mikrobiologie, Fachbereich Biologie and SYNMIKRO, Philipps-Universität, 35032 Marburg, Germany.AbstractElectron bifurcation is a fundamental strategy of energy coupling originally discovered in the Q-cycle of many organisms. Recently a flavin-based electron bifurcation has been detected in anaerobes, first in clostridia and later in acetogens and methanogens. It enables anaerobic bacteria and archaea to reduce the low-potential [4Fe-4S] clusters of ferredoxin, which increases the efficiency of the substrate level and electron transport phosphorylations. Here we characterize the bifurcating electron transferring flavoprotein (EtfAf) and butyryl-CoA dehydrogenase (BcdAf) of Acidaminococcus fermentans, which couple the exergonic reduction of crotonyl-CoA to butyryl-CoA to the endergonic reduction of ferredoxin both with NADH. EtfAf contains one FAD (α-FAD) in subunit α and a second FAD (β-FAD) in subunit β. The distance between the two isoalloxazine rings is 18 Å. The EtfAf-NAD(+) complex structure revealed β-FAD as acceptor of the hydride of NADH. The formed β-FADH(-) is considered as the bifurcating electron donor. As a result of a domain movement, α-FAD is able to approach β-FADH(-) by about 4 Å and to take up one electron yielding a stable anionic semiquinone, α-FAD, which donates this electron further to Dh-FAD of BcdAf after a second domain movement. The remaining non-stabilized neutral semiquinone, β-FADH(•), immediately reduces ferredoxin. Repetition of this process affords a second reduced ferredoxin and Dh-FADH(-) that converts crotonyl-CoA to butyryl-CoA.
The Journal of biological chemistry.J Biol Chem.2014 Feb 21;289(8):5145-57. doi: 10.1074/jbc.M113.521013. Epub 2013 Dec 30.
Electron bifurcation is a fundamental strategy of energy coupling originally discovered in the Q-cycle of many organisms. Recently a flavin-based electron bifurcation has been detected in anaerobes, first in clostridia and later in acetogens and methanogens. It enables anaerobic bacteria and archaea
PMID 24379410

Four Cys residues in heterodimeric 2-oxoacid:ferredoxin oxidoreductase are required for CoA-dependent oxidative decarboxylation but not for a non-oxidative decarboxylation.

Yan Z1, Fushinobu S1, Wakagi T2.Author information 1Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan.2Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan. Electronic address: atwakag@mail.ecc.u-tokyo.ac.jp.AbstractHeterodimeric 2-oxoacid:ferredoxin oxidoreductase (OFOR) from Sulfolobus tokodaii (StOFOR) has only one [4Fe-4S]2+ cluster, ligated by 4 Cys residues, C12, C15, C46, and C197. The enzyme has no other Cys. To elucidate the role of these Cys residues in holding of the iron-sulfur cluster in the course of oxidative decarboxylation of a 2-oxoacid, one or two of these Cys residues was/were substituted with Ala to yield C12A, C15A, C46A, C197A and C12/15A mutants. All the mutants showed the loss of iron-sulfur cluster, except the C197A one which retained some unidentified type of iron-sulfur cluster. On addition of pyruvate to OFOR, the wild type enzyme exhibited a chromophore at 320nm and a stable large EPR signal corresponding to a hydroxyethyl-ThDP radical, while the mutant enzymes did not show formation of any radical intermediate or production of acetyl-CoA, suggesting that the intact [4Fe-4S] cluster is necessary for these processes. The stable radical intermediate in wild type OFOR was rapidly decomposed upon addition of CoA in the absence of an electron acceptor. Non-oxidative decarboxylation of pyruvate, yielding acetaldehyde, has been reported to require CoA for other OFORs, but StOFOR catalyzed acetaldehyde production from pyruvate independent of CoA, regardless of whether the iron-sulfur cluster is intact [4Fe-4S] type or not. A comprehensive reaction scheme for StOFOR with a single cluster was proposed.
Biochimica et biophysica acta.Biochim Biophys Acta.2014 Jan 31;1844(4):736-743. doi: 10.1016/j.bbapap.2014.01.015. [Epub ahead of print]
Heterodimeric 2-oxoacid:ferredoxin oxidoreductase (OFOR) from Sulfolobus tokodaii (StOFOR) has only one [4Fe-4S]2+ cluster, ligated by 4 Cys residues, C12, C15, C46, and C197. The enzyme has no other Cys. To elucidate the role of these Cys residues in holding of the iron-sulfur cluster in the course
PMID 24491525

Role of Azotobacter vinelandii FdxN in FeMo-co biosynthesis.

Jiménez-Vicente E1, Navarro-Rodríguez M1, Poza-Carrión C1, Rubio LM2.Author information 1Centro de Biotecnología y Genómica de Plantas, Universidad Politécnica de Madrid, Pozuelo de Alarcón 28223, Madrid, Spain.2Centro de Biotecnología y Genómica de Plantas, Universidad Politécnica de Madrid, Pozuelo de Alarcón 28223, Madrid, Spain. Electronic address: lm.rubio@upm.es.AbstractBiosynthesis of metal clusters for the nitrogenase component proteins NifH and NifDK involves electron donation events. Yet, electron donors specific to the biosynthetic pathways of the [4Fe-4S] cluster of NifH, or the P-cluster and the FeMo-co of NifDK, have not been identified. Here we show that an Azotobacter vinelandii mutant lacking fdxN was specifically impaired in FeMo-co biosynthesis. The ΔfdxN mutant produced 5-fold less NifB-co, an early FeMo-co biosynthetic intermediate, than wild type. As a consequence, it accumulated FeMo-co-deficient apo-NifDK and was impaired in NifDK activity. We conclude that FdxN plays a role in FeMo-co biosynthesis, presumably by donating electrons to support NifB-co synthesis by NifB. This is the first role in nitrogenase biosynthesis unequivocally assigned to any A. vinelandii ferredoxin.
FEBS letters.FEBS Lett.2014 Jan 31;588(3):512-6. doi: 10.1016/j.febslet.2013.12.018. Epub 2013 Dec 24.
Biosynthesis of metal clusters for the nitrogenase component proteins NifH and NifDK involves electron donation events. Yet, electron donors specific to the biosynthetic pathways of the [4Fe-4S] cluster of NifH, or the P-cluster and the FeMo-co of NifDK, have not been identified. Here we show that a
PMID 24374338

Japanese Journal

2017年度神奈川大学総合理学研究所共同研究助成論文極低温ESRによる金属タンパク質及び金属錯体の機能解析 : 光合成細菌Heliobacillus mobilisのフェレドキシンの性質

羽田野敦史,北島正治,瀬尾悌介,片岡祐介,川本達也,櫻井英博,井上和仁
Science journal of Kanagawa University = 神奈川大学理学誌 29, 93-96, 2018
短報2017年度神奈川大学総合理学研究所共同研究助成論文
NAID 120006707689

Indolepyruvate ferredoxin oxidoreductase : An oxygen-sensitive iron–sulfur enzyme from the hyperthermophilic archaeon Thermococcus profundus

Ozawa Yukiko,Siddiqui Masood Ahmed,Takahashi Yasufumi [他],URUSHIYAMA Akio,OHMORI Daijiro,YAMAKURA Fumiyuki,ARISAKA Fumio,IMAI Takeo
Journal of bioscience and bioengineering 114(1), 23-27, 2012-07-25
Department of Chemistry, Juntendo University
NAID 110009479359

Studies of interaction of homo-dimeric ferredoxin-NAD(P)+ oxidoreductases of Bacillus subtilis and Rhodopseudomonas palustris, that are closely related to thioredoxin reductases in amino acid sequence, with ferredoxins and pyridine nucleotide coenzymes

Seo Daisuke,Okabe Seisuke,Yanase Mitsuhiro,Kataoka Kunishige,Sakurai Takeshi
Biochimica et Biophysica Acta - Proteins and Proteomics 1794(4), 594-601, 2009-04-01
… 金沢大学理工研究域物質化学系Ferredoxin-NADP+ oxidoreductases (FNRs) of Bacillus subtilis (YumC) and Rhodopseudomonas palustris CGA009 (RPA3954) belong to a novel homo-dimeric type of FNR with high amino acid sequence homology to NADPH-thioredoxin reductases. … palustris, [4Fe-4S] type Fd from B. …
NAID 120001088431