Iron-molybdenum cofactor synthesis by a thermophilic nitrogenase devoid of the scaffold NifEN.

The maturation and installation of the active site metal cluster (FeMo-co, FeSCMo--homocitrate) in Mo-dependent nitrogenase requires the protein product of the gene for production of the FeS cluster precursor (NifB-co, [FeSC]) and the action of the maturase complex composed of the protein products from the and genes. However, some putative diazotrophic bacteria, like sp. RS-1, lack the genes, suggesting an alternative pathway for maturation of FeMo-co that does not require NifEN.

Microscale Thermophoresis (MST) as a Tool to Study Binding Interactions of Oxygen-Sensitive Biohybrids.

Microscale thermophoresis (MST) is a technique used to measure the strength of molecular interactions. MST is a -based technique that monitors the change in fluorescence associated with the movement of fluorescent-labeled molecules in response to a temperature gradient triggered by an IR LASER. MST has advantages over other approaches for examining molecular interactions, such as isothermal titration calorimetry, nuclear magnetic resonance, biolayer interferometry, and surface plasmon resonance, requiring a small sample size that does not need to be immobilized and a high-sensitivity fluorescence detection.

The essential malaria protein PfCyRPA targets glycans to invade erythrocytes.

Plasmodium falciparum is a human-adapted apicomplexan parasite that causes the most dangerous form of malaria. P. falciparum cysteine-rich protective antigen (PfCyRPA) is an invasion complex protein essential for erythrocyte invasion.

Hole-scavenging in photo-driven N reduction catalyzed by a CdS-nitrogenase MoFe protein biohybrid system.

The light-driven reduction of dinitrogen (N) to ammonia (NH) catalyzed by a cadmium sulfide (CdS) nanocrystal‑nitrogenase MoFe protein biohybrid is dependent on a range of different factors, including an appropriate hole-scavenging sacrificial electron donor (SED). Here, the impact of different SEDs on the overall rate of N reduction catalyzed by a CdS quantum dot (QD)-MoFe protein system was determined. The selection of SED was guided by several goals: (i) molecules with standard reduction potentials sufficient to reduce the oxidized CdS QD, (ii) molecules that do not absorb the excitation wavelength of the CdS QD, and (iii) molecules that could be readily reduced by sustainable processes.