Narrow Results

Fiber modifications by environmentally friendly processing are essential in order to simplify the preparation and finishing processes, in addition to minimizing the chemical waste and associated disposal problem. In this regard, enzymes have been used extensively because it can remove the small fiber ends from yarn surface to create a smooth fabric surface appearance and introduce a degree of softness without using traditional chemical treatment. However, a significant strength reduction and slow reaction rate of the enzymatic reaction limit its industrial application. In this paper, the potential of using low-temperature plasma (LTP) as a surface pre-treatment prior to enzyme treatment on flax fiber has been studied. By means of the LTP pre-treatment, the effectiveness of enzyme treatment can be enhanced.

Ferrochelatase (also known as PPIX ferrochelatase; Enzyme Commission number 4.9.9.1.1) catalyzes the insertion of ferrous iron into PPIX to form heme. This reaction unites the biochemically synchronized pathways of porphyrin synthesis and iron transport in nearly all living organisms. The ferrochelatases are an evolutionarily diverse family of enzymes with no more than six active site residues known to be perfectly conserved. The availability of over thirty different crystal structures, including many with bound metal ions or porphyrins, has added tremendously to our understanding of ferrochelatase structure and function. It is generally believed that ferrous iron is directly channeled to ferrochelatase in vivo, but the identity of the suspected chaperone remains uncertain despite much recent progress in this area. Identification of a conserved metal ion binding site at the base of the active site cleft may be an important clue as to how ferrochelatases acquire iron, and catalyze desolvation during transport to the catalytic site to complete heme synthesis.

Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX to give heme. Resonance Raman spectroscopy has been instrumental in defining the distortion (mode and extent) of the porphyrin substrate, which is a critical step in the catalytic mechanism of ferrochelatase. Saddling is the predominant porphyrin out-of-plane deformation induced upon binding to ferrochelatase. Our analysis demonstrated that the intensity of the γ₁₅ line, which is assigned to an out-of-plane porphyrin vibration, in resonance Raman spectra obtained for wild-type- and variant ferrochelatase-bound porphyrin, correlates with the saddling deformation undergone by the porphyrin substrate. Further analysis of the three dimensional X-ray structures of bacterial, human and yeast ferrochelatases and the type and extent of distortion of the protein-bound porphyrin substrate and inhibitors using normal structure decomposition, support the view that ferrochelatase catalysis involves binding of a distorted porphyrin substrate and releasing of a flatter, metalated porphyrin.

Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX to generate heme. Despite recent research on the reaction mechanism of ferrochelatase, the precise roles and localization of individual active site residues in catalysis, particularly those involved in the insertion of the ferrous iron into the protoporphyrin IX substrate, remain controversial. One outstanding question is from which side of the macrocycle of the bound porphyin substrate is the ferrous iron substrate inserted. Pre-steady state kinetic experiments done under single-turnover conditions conclusively demonstrate that metal ion insertion is pH-dependent, and that the conserved active site His-Glu pair coordinately catalyzes the metal ion insertion reaction. Further, p$K_a$ calculations and molecular dynamic simulations indicate that the active site His is deprotonated and the protonation state of the Glu relates to the conformational state of ferrochelatase. Specifically, the conserved Glu in the open conformation of ferrochelatase is deprotonated, while it remains protonated in the closed conformation. These findings support not only the role of the His-Glu pair in catalyzing metal ion insertion, as these residues need to be deprotonated to bind the incoming metal ion, but also the importance of the relationship between the protonation state of the Glu residue and the conformation of ferrochelatase. Finally, the results of this study are consistent with our previous proposal that the unwinding of the $\pi$-helix, the major structural determinant of the closed to open conformational transition in ferrochelatase, is associated with the Glu residue binding the Fe${}^{2+}$ substrate from a mitochondrial Fe${}^{2+}$ donor.

This short review highlights the author’s group research on modified vitamin B${}_{12}$ derivatives with a peptide backbone as (1) inhibitors of B${}_{12}$-dependent enzymes and as (2) models of cofactor B${}_{12}$-protein complexes.

The sun is the only source of renewable energy available to us, if geothermal energy is not taken into account. In the form of radiation (UV light, visible light, infrared light, Section 1.1) it sends us annually 178,000 terawatts (1 TW = 10¹² W; unit of power 1 W = 1 J s^–1 = 859.85 calories per hour), that is to say 15,000 times the energy consumed annually by humanity. Only 0.1% of the solar energy received by planet Earth is converted into plant biomass, i.e. 100 × 10⁹ tons per year which corresponds to ca. 180 × 10⁹ tons per year of CO₂ captured from the atmosphere. This CO₂ returns to the biosphere after the death of the plants. Consumption of fossil carbon emits ca. 35 × 10⁹ tons of CO₂ yearly. Biomass is the material produced by all living organisms (plants, animals, microorganisms, fungi)…