about
Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytesNucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coliStructure of Ynk1 from the yeast Saccharomyces cerevisiaeA structural mechanism for dimeric to tetrameric oligomer conversion inHalomonassp. nucleoside diphosphate kinaseCrystal structure of the ribosomal protein S6 from Thermus thermophilusSequence determination of reduction potentials by cysteinyl hydrogen bonds and peptide pipoles in [4Fe-4S] ferredoxins.Ferredoxin and formyltetrahydrofolate synthetase: comparative studies with Clostridium acidiurici, Clostridium cylindrosporum, and newly isolated anaerobic uric acid-fermenting strainsCloning, nucleotide sequence, and transcriptional analyses of the gene encoding a ferredoxin from Methanosarcina thermophila.Structure of ferredoxin I from Azotobacter vinelandiiThe binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin at 2.0-Angstrom resolutionAmino-acid sequence of equine renal metallothionein-1B.Tertiary structure of myohemerythrin at low resolutionSynthetic analogs of active sites of iron-sulfur proteins: bis (o-xylyldithiolato) ferrate (III) monoanion, a structurally unconstrained model for the rubredoxin Fe-S4 unitAerobic inactivation of fumarate reductase from Escherichia coli by mutation of the [3Fe-4S]-quinone binding domainActive photosynthesis in cyanobacterial mutants with directed modifications in the ligands for two iron-sulfur clusters on the PsaC protein of photosystem I.Shared thematic elements in photochemical reaction centersAnalysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio vulgaris Hildenborough.All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly.Sequence of the gene coding for the beta-subunit of dinitrogenase from the blue-green alga AnabaenaCorrelation between rate constant for reduction and redox potential as a basis for systematic investigation of reaction mechanisms of electron transfer proteins.Ferredoxin and ferredoxin-heme maquettes.Synthesis and properties of Clostridium acidi-urici (Leu2)-ferredoxin: a function of the peptide chain and evidence against the direct role of the aromatic residues in electron transfer.NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein.Bacterial iron-sulfur proteins.Open reading frame 5 (ORF5), encoding a ferredoxinlike protein, and nifQ are cotranscribed with nifE, nifN, nifX, and ORF4 in Rhodobacter capsulatus.Nucleotide sequence of the frxB gene in wheat chloroplast DNA.Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins.Mössbauer effect in the eight-iron ferredoxin from Clostridium pasterurianum. Evidence for the state of the iron atomsAmino acid sequence of a four-iron-four-sulphur ferredoxin isolated from Bacillus stearothermophilus.X-ray photoelectron spectra of iron-sulphur proteins.Mössbauer effect in the high-potential iron-sulphur protein from Chromatium. Evidence for the state of the iron atoms.The 18-kD protein that binds to the chloroplast DNA replicative origin is an iron-sulfur protein related to a subunit of NADH dehydrogenase.Electrochemical and spectroscopic characterization of the 7Fe form of ferredoxin III from Desulfovibrio africanus.Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy.Structural Analysis of Cubane-Type Iron Clusters.Modular origins of biological electron transfer chains.Structure of mouse protocadherin 15 of the stereocilia tip link in complex with LHFPL5
P2860
Q24555804-A50CB169-E6A5-43E4-A05F-BD560F10A40BQ24628744-C8F4FF96-EADE-486A-BB83-5E547FA07C3DQ27651056-256C75AD-2621-45B0-A773-65B1E0B567ECQ27676865-A90B38E8-DC9A-436C-97AF-980EC1FA191AQ27731250-CD75CF65-E43F-49FE-823C-30270BB9A6CCQ28344473-E20FDB70-E2A1-46A1-91D4-D72DC91F9B82Q28776770-8811FD7C-60D8-42B2-BEB4-C4DAD7956A96Q30990332-8589A7C8-62FF-4DDD-A1CE-69B603B7282BQ33552312-B8C15F6F-1658-4F85-B62D-A91130F4A6CFQ34753524-5B841AB3-43F9-4F8E-BFB9-04DD92C2F898Q35029522-6B3067C0-0C4A-4D1A-B7C9-914EEBC999BDQ35081202-BE4F8631-ECB9-49B7-8A44-8745EF79D304Q35084622-3373986B-A305-4712-80CA-696F85E8ED7EQ35592151-6D3EB710-3A8B-445C-95EC-DABE09778E81Q35847907-E11F47D4-ED12-4C73-B205-3E5952A3DE53Q36121807-7669DBDA-B3E9-445F-9477-6D07505B1BEFQ36181794-923F23B4-C296-4322-9980-E2D3A742BC40Q36281126-DF62AD53-6B36-4DB0-9F1E-1A2D08E75BBCQ36320044-46477622-7FBC-410C-ADC5-445E7B4E70D7Q36615135-554BDBEF-196B-4B57-8388-E4711009F18CQ37082287-43E2D7BF-AC30-4473-BD0E-E715C217F503Q37439434-0F065B60-8662-4F32-B1DF-E143AC68C07AQ37464163-1DCAA054-8338-4862-9091-19CAE1F08BAEQ38065974-2F9F2652-F3B7-4062-B649-C2247F9D5A7AQ39948839-3A2A44E4-98F9-4667-A692-D3D78A793179Q40536474-47DF84B2-BA6C-445D-80F3-A219E153A510Q41827158-457CA6DD-0A5C-4E97-BBD6-FE020B16D3C2Q41920278-7FF38366-69A5-48BE-8B1F-20EBB1C56961Q42170425-78050814-08DC-4092-8BC1-C9A3FAF57272Q42555370-749690F1-13CE-4694-B075-325C46190D1FQ42561738-26234ADA-DB18-4969-9B13-B01F62E0502AQ42642647-E7AA3D47-ECE5-42DB-91D3-46ED937D6148Q42804669-B048A1E7-6B3B-4061-914C-6A53E52A5D43Q42841839-EF576424-983F-4BC0-8B9B-6A03E04CA66AQ42971570-2A01A233-12FC-4A1A-AE34-34027837CA91Q49874078-4A4F7BF6-DA75-45A0-9016-D666A9D38359Q56530447-781004E1-AE52-4D21-B10C-EC4F8A4018EA
P2860
description
1973 nî lūn-bûn
@nan
1973年の論文
@ja
1973年学术文章
@wuu
1973年学术文章
@zh
1973年学术文章
@zh-cn
1973年学术文章
@zh-hans
1973年学术文章
@zh-my
1973年学术文章
@zh-sg
1973年學術文章
@yue
1973年學術文章
@zh-hant
name
Structure of a bacterial ferredoxin.
@en
Structure of a bacterial ferredoxin.
@nl
type
label
Structure of a bacterial ferredoxin.
@en
Structure of a bacterial ferredoxin.
@nl
prefLabel
Structure of a bacterial ferredoxin.
@en
Structure of a bacterial ferredoxin.
@nl
P2093
P1476
Structure of a bacterial ferredoxin
@en
P2093
P304
P407
P577
1973-06-01T00:00:00Z