Nanoclusters and nanolines: the effect of molybdenum oxide substrate stoichiometry on iron self-assembly

The growth of Fe nanostructures on the stoichiometric MoO₂/Mo(110) and oxygen-rich MoO₂+x /Mo(110) surfaces has been studied using low-temperature scanning tunnelling microscopy (STM) and density functional theory calculations. STM results indicate that at low coverage Fe nucleates on the MoO₂/Mo(110) surface, forming small, well-ordered nanoclusters of uniform size, each consisting of five Fe atoms. These five-atom clusters can agglomerate into larger nanostructures reflecting the substrate geometry, but they retain their individual character within the structure. Linear Fe nanocluster arrays are formed on the MoO₂/Mo(110) surface at room temperature when the surface coverage is greater than 0.6 monolayers. These nanocluster arrays follow the direction of the oxide rows of the strained MoO₂/Mo(110) surface. Slightly altering the preparation procedure of MoO₂/Mo(110) leads to the presence of oxygen adatoms on this surface. Fe deposition onto the oxygen-rich MoO₂+x /Mo(110) surface results in elongated nanostructures that reach up to 24 nm in length. These nanolines have a zigzag shape and are likely composed of partially oxidised Fe formed upon reaction with the oxygen-rich surface

The Elusive Third Subunit IIa of the Bacterial B-Type Oxidases: The Enzyme from the Hyperthermophile Aquifex aeolicus

The reduction of molecular oxygen to water is catalyzed by complicated membrane-bound metallo-enzymes containing variable numbers of subunits, called cytochrome c oxidases or quinol oxidases. We previously described the cytochrome c oxidase II from the hyperthermophilic bacterium Aquifex aeolicus as a ba3-type two-subunit (subunits I and II) enzyme and showed that it is included in a supercomplex involved in the sulfide-oxygen respiration pathway. It belongs to the B-family of the heme-copper oxidases, enzymes that are far less studied than the ones from family A. Here, we describe the presence in this enzyme of an additional transmembrane helix “subunit IIa”, which is composed of 41 amino acid residues with a measured molecular mass of 5105 Da. Moreover, we show that subunit II, as expected, is in fact longer than the originally annotated protein (from the genome) and contains a transmembrane domain. Using Aquifex aeolicus genomic sequence analyses, N-terminal sequencing, peptide mass fingerprinting and mass spectrometry analysis on entire subunits, we conclude that the B-type enzyme from this bacterium is a three-subunit complex. It is composed of subunit I (encoded by coxA2) of 59000 Da, subunit II (encoded by coxB2) of 16700 Da and subunit IIa which contain 12, 1 and 1 transmembrane helices respectively. A structural model indicates that the structural organization of the complex strongly resembles that of the ba3 cytochrome c oxidase from the bacterium Thermus thermophilus, the IIa helical subunit being structurally the lacking N-terminal transmembrane helix of subunit II present in the A-type oxidases. Analysis of the genomic context of genes encoding oxidases indicates that this third subunit is present in many of the bacterial oxidases from B-family, enzymes that have been described as two-subunit complexes