about
Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandiiVnfY is required for full activity of the vanadium-containing dinitrogenase in Azotobacter vinelandiiCloning and mutational analysis of the gamma gene from Azotobacter vinelandii defines a new family of proteins capable of metallocluster binding and protein stabilization.Maturation of nitrogenase: a biochemical puzzleMolybdenum trafficking for nitrogen fixationA sterile alpha-motif domain in NafY targets apo-NifDK for iron-molybdenum cofactor delivery via a tethered domainNifB and NifEN protein levels are regulated by ClpX2 under nitrogen fixation conditions in Azotobacter vinelandii.In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteinsHydrogen overproducing nitrogenases obtained by random mutagenesis and high-throughput screening.Formation of Nitrogenase NifDK Tetramers in the Mitochondria of Saccharomyces cerevisiae.Expression of a functional oxygen-labile nitrogenase component in the mitochondrial matrix of aerobically grown yeast.Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized to support diverse anaerobic metabolic processesExtended X-ray absorption fine structure and nuclear resonance vibrational spectroscopy reveal that NifB-co, a FeMo-co precursor, comprises a 6Fe core with an interstitial light atom.Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer.Electron Paramagnetic Resonance Characterization of Three Iron-Sulfur Clusters Present in the Nitrogenase Cofactor Maturase NifB from Methanocaldococcus infernus.EXAFS reveals two Mo environments in the nitrogenase iron-molybdenum cofactor biosynthetic protein NifQ.Purification and In Vitro Activity of Mitochondria Targeted Nitrogenase Cofactor Maturase NifBKinetics of Nif gene expression in a nitrogen-fixing bacterium.Expression and purification of NifB proteins from aerobic and anaerobic sources.Substrate specificity and evolutionary implications of a NifDK enzyme carrying NifB-co at its active site.Purification of a NifEN protein complex that contains bound molybdenum and a FeMo-Co precursor from an Azotobacter vinelandii DeltanifHDK strain.Evidence for nifU and nifS participation in the biosynthesis of the iron-molybdenum cofactor of nitrogenase.Identification of a Mo-Fe-S cluster on NifEN by Mo K-edge extended X-ray absorption fine structure.NifX and NifEN exchange NifB cofactor and the VK-cluster, a newly isolated intermediate of the iron-molybdenum cofactor biosynthetic pathway.NAD-, NMN-, and NADP-dependent modification of dinitrogenase reductases from Rhodospirillum rubrum and Azotobacter vinelandii.New insights into the mechanism of nickel insertion into carbon monoxide dehydrogenase: analysis of Rhodospirillum rubrum carbon monoxide dehydrogenase variants with substituted ligands to the [Fe3S4] portion of the active-site C-cluster.Diversity and Functional Analysis of the FeMo-Cofactor Maturase NifB.State of the Art in Eukaryotic Nitrogenase Engineering.Adaptation of the GoldenBraid modular cloning system and creation of a toolkit for the expression of heterologous proteins in yeast mitochondria.Tuning a nitrate reductase for function. The first spectropotentiometric characterization of a bacterial assimilatory nitrate reductase reveals novel redox properties.Molybdopterin guanine dinucleotide cofactor in Synechococcus sp. nitrate reductase: identification of mobA and isolation of a putative moeB gene.The Nitrogenase FeMo-Cofactor Precursor Formed by NifB Protein: A Diamagnetic Cluster Containing Eight Iron Atoms.Enzyme-catalysed nitrate reduction-themes and variations as revealed by protein film voltammetry.Role of Azotobacter vinelandii FdxN in FeMo-co biosynthesis.Purification, cofactor analysis, and site-directed mutagenesis of Synechococcus ferredoxin-nitrate reductase.A cyanobacterial narB gene encodes a ferredoxin-dependent nitrate reductaseThe Nitrogenase FeMo-Cofactor Precursor Formed by NifB Protein: A Diamagnetic Cluster Containing Eight Iron AtomsPurification of O2-sensitive metalloproteinsCorrigendum to "Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer" [Plant Sci. 225 (August) (2014) 130-137]Biosynthesis of the nitrogenase active-site cofactor precursor NifB-co in Saccharomyces cerevisiae
P50
Q24524115-6ABDB4FB-4F22-48DC-B5CE-B35287B441F3Q24554263-21B76135-19BF-4797-8457-1078577FF8EAQ30671302-389E936A-3C58-4952-95B5-426487C5F9B3Q33340714-072634C9-9958-4036-8222-44463B0EE7D8Q34393472-4302F50C-FB59-47A2-85AE-289EC01884B7Q34675999-FE6A356A-622F-4D8E-A1B9-CF4EEBE93D77Q35016407-14CE8475-12CA-4F9A-96CA-BB14E88C78BFQ36140870-6E4ED1DD-53F1-457F-9A9F-5EFA8DE79218Q36211595-C4E15399-21B3-4155-ACCA-F6CD92868C79Q36286077-F5CA5B12-8B09-46B9-BD9E-EC38BA46E58AQ36865886-17FA33BF-E130-440E-AB6C-65A92F2047BAQ37247836-F3CEF2E1-816E-478C-A73D-F21FB76EADA5Q37326127-4F0FEDA6-D3FC-4DE4-B68B-D0B0B29F98A0Q38228815-FC193C71-FA87-4D12-BB5C-02269C3C5742Q41411497-C37326C6-A801-400E-AE6B-21597D422BE5Q41440680-9A860B21-F987-4BE4-B20C-B22574865C4DQ41684619-F69192C3-CAA9-435E-8FCA-C124E44BA033Q41908212-D32AC14C-8960-4EDE-8DD0-22C5EC84550AQ43021165-B78FD893-98EC-4403-9CBE-14F3049B71D5Q43135047-303767A5-3515-43A0-BB35-80756701EF06Q44317068-B831CC05-4C58-4C75-91E7-A92909965D6CQ45975733-371A98A2-C291-4DBE-9C1A-445007228E69Q45992257-DEEC5EE2-ED13-40BB-AA5E-6EB8FBD9D430Q46322584-047A3109-8B15-4125-956B-9F9B5799C519Q46753592-CE7199A2-E49F-4E7C-BA71-C30B811F69AAQ46800581-3C022A20-7F2E-482F-870D-2058ACF65C9DQ47115775-F339F231-A3A8-4563-AA9B-879BD371691AQ47249748-CD176A86-A8B7-43D6-9CDB-37FD4D06C471Q47353731-B657DC91-F21C-4712-8335-C17D83B522C8Q47421937-8274224B-BDF6-48E4-A5CA-D270C29D7E38Q47895220-12F4583D-C986-43A2-9FC2-499CAB817A1FQ48362349-AB7A6DDA-8072-42F6-855D-2BD4DE3FA9E1Q51717137-01B23705-69CB-4DAE-BAB6-40D65B1C0907Q54389972-D7EABE83-2840-4765-AEDF-7CDA5EFF991BQ54477293-61798748-951A-478B-8E62-0A8129E53E4CQ61221580-6F227300-9D3F-4649-BB98-304597EBEE39Q63987564-8E50CCE2-AB3B-45C1-B1DB-8344E41AE259Q87462389-5B8B7550-1478-468B-ABB5-DBF252CA034DQ88175451-405969BA-DE5D-4040-9CA9-7540741FE0ACQ91450999-C44CFAA2-A171-4CFC-913F-C7F67F2B12A0
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Luis M Rubio
@es
Luis M Rubio
@fr
Luis M Rubio
@sl
Luis M. Rubio
@en
type
label
Luis M Rubio
@es
Luis M Rubio
@fr
Luis M Rubio
@sl
Luis M. Rubio
@en
prefLabel
Luis M Rubio
@es
Luis M Rubio
@fr
Luis M Rubio
@sl
Luis M. Rubio
@en
P1053
B-5827-2009
P106
P1153
35278523000
P21
P31
P3829
P496
0000-0003-1596-2475