Structure and mechanical properties of stainless-steel specimens, made by additive method, after pulsed electron beam treatment

The article presents a method for finishing the surface of metal products made by sequential electron-beam surfacing, which consists in modifying the surface with an intense low-energy electron beam of submillisecond duration. On the example of 308LSi stainless steel, the results of such processing are demonstrated, the optimal modes of exposure are determined. It is shown that as a result of pulsed electron-beam processing, a homogeneous polycrystalline structure without cracks is formed on the surface with unchanged, relative to the initial material, elemental composition, strength (microhardness) and tribological (wear rate) properties. In this case, the surface roughness is reduced to 2.1 times in the longitudinal direction relative to the surfacing plane, to 5.2 times in the transverse direction. Tensile tests of specimens showed anisotropy of mechanical properties depending on the direction of tension relative to the surfacing plane, which decreases after surface pulse electron-beam processing.

Substrate recognition induces sequential electron transfer across subunits in the nitrogenase-like DPOR complex

A key step in bacteriochlorophyll biosynthesis is the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide), catalyzed by dark-operative protochlorophyllide oxidoreductase (DPOR). DPOR is made of electron donor (BchL) and acceptor (BchNB) component proteins. BchNB is further composed of two subunits each of BchN and BchB arranged as an α2β2 heterotetramer with two active sites for substrate reduction. Such oligomeric architectures are found in several other electron transfer (ET) complexes, but how this architecture influences activity is unclear. Here, we describe allosteric communication between the two identical active sites in Rhodobacter sphaeroides BchNB that drives sequential and asymmetric ET. Pchlide binding to one BchNB active site initiates ET from the pre-reduced [4Fe-4S] cluster of BchNB, a process similar to the deficit spending mechanism observed in the structurally related nitrogenase complex. Pchlide binding in one active site is recognized in trans by an Asp-274 from the opposing half, which is positioned to serve as the initial proton donor. A D274A variant DPOR binds to two Pchlide molecules in the BchNB complex, but only one is bound productively, stalling Pchlide reduction in both active sites. A half-active complex combining one WT and one D274A monomer also stalled after one electron was transferred in the WT half. We propose that such sequential electron transfer in oligomeric enzymes serves as a regulatory mechanism to ensure binding and recognition of the correct substrate. The findings shed light on the functional advantages imparted by the oligomeric architecture found in many electron transfer enzymes.