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x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
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x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
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x * 18000, HoxE, SDS-PAGE, x * 21000, recombinant HIs-tagged HoxE, SDS-PAGE
hexamer
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subunit stoichiometry of HoxFUYI2. Subunit HoxIhas a MW of 19000 Da as determined by SDS-PAGE
hexamer
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subunit stoichiometry of HoxFUYI2. Subunit HoxIhas a MW of 19000 Da as determined by SDS-PAGE
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oligomer
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enzyme is composed as a dimer of pentamers, the latter consisting of subunit pairs HoxU with HoxF, and HoxY with HoxH, and a fifth 19 kDa subunit HoxI, i.e. B protein, the HoxFU dimer is the NADH-dehydrogenase moiety, the HoxHY dimer is the hydrogenase moiety, overview
oligomer
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heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities, subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity with 56 kDa for HoxH and 26 kDa for HoxY, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase, i.e. diaphorase activity
oligomer
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enzyme is composed as a dimer of pentamers, the latter consisting of subunit pairs HoxU with HoxF, and HoxY with HoxH, and a fifth 19 kDa subunit HoxI, i.e. B protein, the HoxFU dimer is the NADH-dehydrogenase moiety, the HoxHY dimer is the hydrogenase moiety, overview
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oligomer
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heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities, subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity with 56 kDa for HoxH and 26 kDa for HoxY, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase, i.e. diaphorase activity
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tetramer
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1 * 65000 + 1 * 64000 + 1 * 20000 + 1 * 14000, SDS-PAGE
tetramer
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1 * 67000 + 1 * 55000 + 1 * 26000 + 1 * 23000
tetramer
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enzyme is composed of 4 Hox subunits, HoxF, HoxH, HoxU, and HoxY, with MWs of 67 kDa, 55 kDa, 26 kDa, and 23 kDa
tetramer
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the catalytic subunit is termed HoxH
tetramer
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1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
tetramer
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1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
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additional information
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enzyme is composed of 4 subunits
additional information
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enzyme is composed of 4 subunits
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additional information
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enzyme is composed of 4 subunits
additional information
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structure analysis and subunit composition, HoxI is associated with the NADH-dehydrogenase moiety of the enzyme
additional information
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subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase or diaphorase activity
additional information
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use of a reverse micelle system for study of oligomeric structure
additional information
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structure analysis and subunit composition, HoxI is associated with the NADH-dehydrogenase moiety of the enzyme
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additional information
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use of a reverse micelle system for study of oligomeric structure
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additional information
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large dimer composed of 64000 Da and 31000 Da subunit contains 1 FMN, 1 [2Fe-2S] and 2 [4Fe-4S] cluster, diaphorase activity is located on large dimer, small dimer composed of 56000 Da and 27000 Da subunits contains 2 Ni and 1 [4Fe-4S]/[3Fe-xS] cluster, hydrogenase activity is localized on small dimer
additional information
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enzyme is composed of 4 subunits
additional information
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in low-salt buffer the tetrameric enzyme dissociates into 2 dimeric forms accompanied by the failure to reduce NAD+
additional information
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large dimer composed of 64000 Da and 31000 Da subunit contains 1 FMN, 1 [2Fe-2S] and 2 [4Fe-4S] cluster, diaphorase activity is located on large dimer, small dimer composed of 56000 Da and 27000 Da subunits contains 2 Ni and 1 [4Fe-4S]/[3Fe-xS] cluster, hydrogenase activity is localized on small dimer
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additional information
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in low-salt buffer the tetrameric enzyme dissociates into 2 dimeric forms accompanied by the failure to reduce NAD+
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additional information
the subunit HoxE, which is essential for the bidirectional hydrogenase activity, is included in a pentameric bidirectional hydrogenase complex HoxEFUYH in cyanobacteria, the complex forms dimer (HoxEFUYH)2, complex components are HoxE, HoxF, HoxH, HoxU, and HoxY, complex composition analysis, overview
additional information
the subunit HoxE, which is essential for the bidirectional hydrogenase activity, is included in a pentameric bidirectional hydrogenase complex HoxEFUYH of the cyanobacterial-type, complex components are HoxE, HoxF, HoxH, HoxU, and HoxY
additional information
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the subunit HoxE, which is essential for the bidirectional hydrogenase activity, is included in a pentameric bidirectional hydrogenase complex HoxEFUYH of the cyanobacterial-type, complex components are HoxE, HoxF, HoxH, HoxU, and HoxY