1.8.7.3	?	x * 18000, subunit HdrC2, SDS-PAGE	743210	
1.8.7.3	?	x * 33000, subunit HdrB2, SDS-PAGE	743210	
1.8.7.3	additional information	the HdrABC subunits have different catalytic activities and contain the cofactors that comprise the electron-transferring conduits and heterodisulfide binding site, and facilitate the bifurcation of electrons from the sole flavin adenine dinucleotide (FAD) molecule in HdrA	-, 764472	
1.8.7.3	additional information	three-dimensional map and model of the dimeric Fdh-Hdr-Fmd complex, its active sites, and Fe-S cluster relay. The structure of the D3-hexameric complex is made by threefold repetition of the dimeric structure, and contains dimeric organization of Hdr and Fmd subunits. Mass spectrometry reveals that the Fdh-Hdr-Fmd complex elutes from gel filtration primarily as a 1-MDa dimer of subunits FdhAB-MvhD-HdrABCFmdABCDFG. The Fdh-Hdr complexes are isolated as two oligomeric states, which contain FdhAB-MvhD-HdrABCFmdF. Two of five isoenzymes of FdhA and are detected in all complexes	765833	
1.8.7.3	oligomer	structure analysis of the native heterododecameric HdrABC-MvhAGD complex, overview. The multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached	-, 765831	
1.8.7.3	oligomer	structure analysis of the native heterododecameric HdrABC-MvhAGD complex, overview. The multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached. HdrA is tightly associated with HdrA' (amino acid residues of the partner protomer are marked with an apostrophe) and comprises anN-terminal (1 to 133), a thioredoxin-reductase (145 to 236 and 315 to 567), an inserted ferredoxin (237 to 314), and a C-terminal ferredoxin domain (568 to 654)	-, 765831	
1.8.7.3	oligomer	the multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached	765831