Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions - Test2 - elhamkhani - TriplyDB

Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions

Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions

http://www.wikidata.org/entity/Q24680072

about

Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis The antiviral protein viperin is a radical SAM enzyme Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme Mechanistic and functional versatility of radical SAM enzymes RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA The Radical S-Adenosyl-L-methionine Enzyme QhpD Catalyzes Sequential Formation of Intra-protein Sulfur-to-Methylene Carbon Thioether Bonds Structures of lipoyl synthase reveal a compact active site for controlling sequential sulfur insertion reactions Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion Radical SAM enzymes in methylation and methylthiolation Subunit structure of benzylsuccinate synthase.Adenosyl radical: reagent and catalyst in enzyme reactions.The biosynthesis of thiol- and thioether-containing cofactors and secondary metabolites catalyzed by radical S-adenosylmethionine enzymes.Probing the reaction mechanism of spore photoproduct lyase (SPL) via diastereoselectively labeled dinucleotide SP TpT substrates.Biotin in microbes, the genes involved in its biosynthesis, its biochemical role and perspectives for biotechnological production.Covalent intermediate in the catalytic mechanism of the radical S-adenosyl-L-methionine methyl synthase RlmN trapped by mutagenesis.Response to iron deprivation in Saccharomyces cerevisiae.Regulation of cation balance in Saccharomyces cerevisiae Cofactor dependence of reduction potentials for [4Fe-4S]2+/1+ in lysine 2,3-aminomutase.RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli.Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme Cysteine methylation controls radical generation in the Cfr radical AdoMet rRNA methyltransferase Anaerobic functionalization of unactivated C-H bonds.Control of radical chemistry in the AdoMet radical enzymes Characterization and mechanistic studies of DesII: a radical S-adenosyl-L-methionine enzyme involved in the biosynthesis of TDP-D-desosamine.Transcriptional analysis of biofilm formation processes in the anaerobic, hyperthermophilic bacterium Thermotoga maritima.Radical S-adenosylmethionine enzymes.Structural insights into radical generation by the radical SAM superfamily.Closing in on complete pathways of biotin biosynthesis.Role of the [2Fe-2S]2+ cluster in biotin synthase: mutagenesis of the atypical metal ligand arginine 260 Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB.Into the Wild: Parallel Transcriptomics of the Tsetse-Wigglesworthia Mutualism within Kenyan Populations.Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli.Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase Control of adenosylmethionine-dependent radical generation in biotin synthase: a kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB.Reduction of the [2Fe-2S] cluster accompanies formation of the intermediate 9-mercaptodethiobiotin in Escherichia coli biotin synthase.Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217.A complex between biotin synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly.Reductive cleavage of S-adenosylmethionine by biotin synthase from Escherichia coli.Loss of iron-sulfur clusters from biotin synthase as a result of catalysis promotes unfolding and degradation.Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima.

P2860

Q24295080-EDE022C7-6273-4D5F-8F6F-A479DA8EB2D9 Q24300516-6B268F1E-E41D-429C-9DD4-06474E60DAEB Q24545773-7614C0C7-8CA4-421D-BA9A-E330302A759D Q24631359-FEE3AFC3-3DC3-4D3A-B250-B17536C858FC Q24632475-4059D216-3B48-427B-A364-46DD0C8DD7A9 Q27313394-CFA6CA0E-1DD5-46F8-8538-A39163A4960B Q27694727-A99F7B67-977A-4FFA-8518-39826F9A4927 Q28343711-7876187F-2E5F-4211-9D1D-1B987A74B18A Q33575267-AD42E6D2-92E1-4063-B66A-927295AE94B5 Q33645569-4B6874D0-88FF-43AC-9EBC-EB1E802C3CE5 Q34447149-CC0995E6-D0A3-4080-A427-558D650E12C2 Q35080219-A5B922EB-733C-4C7F-A16B-0B4A998716F7 Q35091451-BA044D3D-8370-43DC-8624-33556EB46459 Q35092677-A4517C1A-1E15-4DBA-A419-CB03DCFCABA0 Q36402114-857CC8AE-03B0-4E7D-AA23-5777E5F89198 Q36423342-97D1AF72-A76F-405A-A776-5FDFE70C3D48 Q36643830-8E37A661-A3B0-4164-A59B-9EDDE0B8428B Q36866933-A1FB7BC1-C598-4612-ACA1-2E67C452295D Q36882918-A018ECA8-F8ED-4EA5-B1E2-D5A32F642F50 Q36908654-DF4B0136-B965-4FB7-943C-A5A630B6F1E2 Q36986036-688B03FA-B90D-4A7D-B8AB-3E294EF214A7 Q37388852-24B62752-7C28-4EF8-BE0E-A8C242441DC2 Q37408927-BE43EBBF-A237-4FF0-B87D-2473F2C3A089 Q37428614-957607C8-34C1-4EA3-BB22-B26C05E8ACAE Q37572285-B35756B8-9919-4F41-AD13-DCABDC551C95 Q37727698-E38B78A0-8879-4966-8925-3C16416D222F Q37849296-D103EBA2-6D7D-4F78-8104-C9AE43A18CCA Q37857719-1713EEFE-8619-4181-AC0C-46585C3FDE7E Q39660280-FF339595-0F42-49C4-B1F5-01C38107B3EA Q39677839-0DB3BEAC-2294-40F0-83D5-A44680DE0354 Q41692208-94A93C4C-F2D6-458D-A6CA-964F892A7F3E Q41821143-7E825799-82D6-4546-8D33-9369144B7DED Q41839348-E7E3FD6B-4B05-45FB-B177-0A856AC8C9F1 Q41853708-0F630E93-C001-4513-A37D-194DF4131FA0 Q41884566-CF1B6855-DF64-4FA4-811D-0E30E9409D50 Q41998819-6AB98AF5-AC5B-4D90-AB85-D2F1184BBD8D Q42069948-DF5C4559-1FAC-4B8E-AEFB-59B7999FABFE Q42162251-80F1D231-03FD-4EE4-840A-BB71A7ECED60 Q43013624-61CBBBC3-0E21-4A46-A9FE-45695EC62694 Q43018092-759EC185-CDF5-4978-B3A9-3AA373BE265E

P2860

Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions

http://www.wikidata.org/entity/Q24680072

description

2001 nî lūn-bûn

@nan

2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Biotin synthase contains two d ...... ulfur cluster interconversions

@ast

Biotin synthase contains two d ...... ulfur cluster interconversions

@en

Biotin synthase contains two d ...... ulfur cluster interconversions

@nl

type

label

Biotin synthase contains two d ...... ulfur cluster interconversions

@ast

Biotin synthase contains two d ...... ulfur cluster interconversions

@en

Biotin synthase contains two d ...... ulfur cluster interconversions

@nl

prefLabel

Biotin synthase contains two d ...... ulfur cluster interconversions

@ast

Biotin synthase contains two d ...... ulfur cluster interconversions

@en

Biotin synthase contains two d ...... ulfur cluster interconversions

@nl

P1433

Q24680072-CDE18814-152E-4385-8CA7-C257B4ACBEAB

P1476

Q24680072-8C5009A9-0611-4417-B9E0-744E1F1B8C9A

P2093

Q24680072-082C4C08-AE99-4C35-A78B-3D04B463B838

Q24680072-3DF52507-2A75-4371-862C-801A19C68BCF

Q24680072-ABA3E2D1-E6B3-4F7B-B949-C5A7EC37AE76

P2860

Q24680072-02DC50B8-FF73-4632-A0D7-BE2C6B38D017

Q24680072-16A80109-251E-4148-BC1F-27DDFDF1CD90

Q24680072-1A9770F8-3D81-4219-80E2-F8F920DAB0CE

Q24680072-21FA0DF9-876A-4FF0-A694-E80BA855AE39

Q24680072-27191870-8A33-49D7-8A94-3C715806214C

Q24680072-40CF18D1-08F4-4D81-8016-A521B3E74F66

Q24680072-45EDA80B-964D-4305-ACC2-0CBD64B4711A

Q24680072-4AED430D-EF85-4031-A0AE-A18499060231

Q24680072-4FC92A3F-CF01-4562-907B-ADFB374ADC16

Q24680072-663B0480-1C85-4936-84D6-142BDD73DD31

P304

Q24680072-75980718-54DE-476C-BF1B-CB91407CFF01

P31

Q24680072-B5C57E33-1D87-4189-B5F6-33E37CE1F9FB

P356

Q24680072-A81035AA-16ED-4690-B321-45A3F5C94068

P407

Q24680072-CB2003F1-9042-463A-A076-83A238C56152

P433

Q24680072-557D0B8B-74AE-4AC8-9462-8473BA2E3F2E

P478

Q24680072-6B2D7074-93F3-4278-86C2-CA8CBE1C3F79

P577

Q24680072-44696A8A-3E4F-4C50-BBC0-E80D748FFE9A

P5875

Q24680072-B0E21827-E000-4666-8625-993256694312

P698

Q24680072-C3269897-542C-4F87-876F-9E49E7559EAB

P932

Q24680072-34C3F413-6157-45DB-87FD-43A2E94E5BD6

P356

P1433

P1476

Biotin synthase contains two d ...... ulfur cluster interconversions

@en

P2093

B R Gibney

http://www.w3.org/2001/XMLSchema#string

J T Jarrett

http://www.w3.org/2001/XMLSchema#string

N B Ugulava

http://www.w3.org/2001/XMLSchema#string

P2860

Deletion and complementation analysis of biotin gene cluster of Escherichia coli

Genetic and biochemical analysis of the biotin loci of Escherichia coli K-12

Iron-sulfur cluster cysteine-to-serine mutants of Anabaena -2Fe-2S- ferredoxin exhibit unexpected redox properties and are competent in electron transfer to ferredoxin:NADP+ reductase

Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion

Lysine 2,3-aminomutase from Clostridium subterminale SB4: mass spectral characterization of cyanogen bromide-treated peptides and cloning, sequencing, and expression of the gene kamA in Escherichia coli.

Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein.

Biochemical and genetic characterization of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism.

Iron-sulfur clusters/semiquinones in complex I.

Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli.

Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin?

P304

8343-51

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/BI0104625

http://www.w3.org/2001/XMLSchema#string

P407

P433

28

http://www.w3.org/2001/XMLSchema#string

P478

40

http://www.w3.org/2001/XMLSchema#string

P577

2001-07-27T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11896403

http://www.w3.org/2001/XMLSchema#string

P698

11444981

http://www.w3.org/2001/XMLSchema#string

P932

1538964

http://www.w3.org/2001/XMLSchema#string