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Microalgae for Pigments and Cosmetics
Published in Sanjeet Mehariya, Shashi Kant Bhatia, Obulisamy Parthiba Karthikeyan, Algal Biorefineries and the Circular Bioeconomy, 2022
Nídia S. Caetano, Priscila S. Corrêa, Wilson G. de Morais Júnior, Gisela M. Oliveira, António A.A. Martins, Teresa M. Mata, Monique Branco-Vieira
The chlorophyll biosynthesis can be divided into two different pathways. The first step is the biosynthesis of chlorophyll and heme precursor, called protoporphyrin IX. This compound is synthesized from the ALA at the stroma of the chloroplast. The second step is the conversion of protoporphyrin IX into chlorophyllide, the precursor of Chl a and Chl b (Figure 5.1). Chl a and Chl b share the same biosynthetic pathway, differing on the transformation of the methyl group in Chl a and an aldehyde group in Chl b (Willows, 2007).
Surface-Enhanced Spectro-Electrochemistry of Biological and Molecular Catalysts on Plasmonic Electrodes
Published in Marc Lamy de la Chapelle, Nordin Felidj, Plasmonics in Chemistry and Biology, 2019
Patrycja Kielb, Inez M. Weidinger
A variety of enzymatic catalysts are based on metal–porphyrins and their abundance has a great impact in a variety of life-sustaining reactions. The most known protein cofactors with incorporated porphyrins are hemes. Biosynthesis of all hemes in a cell begins from the formation of protoporphyrin IX, which structure is depicted in Fig. 5.3 [3]. The porphyrin macrocycle consists of four pyrrole rings connected to each other by methine bridges. Such a structure allows the incorporation of different metal atoms, which are coordinated by four pyrrolic nitrogens [4].
Tests on Naturally Voided Body Fluids
Published in Robert B. Northrop, Non-Invasive Instrumentation and Measurement in Medical Diagnosis, 2017
In PCT, the deficient enzyme is uroporphyrinogen decarboxylase. In EPP, the deficient enzyme is ferrochelatase, which places Fe++ in the heme ring. In EPP, there is a build-up of protoporphyrin IX in bone marrow and erythrocytes. This excess protoporphyrin enters the plasma, and is excreted by the liver into bile and feces.
Endocrine disrupting chemicals (EDCs): chemical fate, distribution, analytical methods and promising remediation strategies – a critical review
Published in Environmental Technology Reviews, 2023
Mridula Chaturvedi, Sam Joy, Rinkoo Devi Gupta, Sangeeta Pandey, Shashi Sharma
Manganese peroxidase (MnP) is an extracellular enzyme containing an iron protoporphyrin IX (heme) prosthetic group, which uses Mn2+ as the electron donor MnP is a glycoprotein with molecular weights ranging from 38 to 62.5 kD, pH optima of 4–7 and temperature optima of 40–60°C. The secretion and synthesis of manganese peroxidases are very much influenced by the culture conditions, fungal developmental state, nutrient levels (N/C ratio) and the addition of inducer to the culture medium [166]. The activity of enzyme is inhibited by Hg2+, Pb2+, Ag+, lactate, NaN3, CaCl2, TEMED, ascorbic acid and beta-mercaptoethanol. Oxalate, malonate and lactate are some of the carboxylic acid chelators, oxalate being the most common one [167].
Low toxicity and high efficacy in use of novel approaches to control Aedes aegypti
Published in Journal of Toxicology and Environmental Health, Part B, 2020
Vanessa Santana Vieira Santos, Boscolli Barbosa Pereira
Specifically, Neris et al. (2018) noted that porphyrins exhibit a potential broad-spectrum effectiveness in the treatment of different enveloped viruses, including Zika and Chikungunya viral particles. Lab bioassays revealed viral envelope protein loss induced by porphyrin, which consequently affected viral morphology, adsorption and entry into target cells (Neris et al. 2018). In addition, porphyrins exerted modulatory effects on heme oxygenase activity and the ability to generate reactive oxygen species (ROS) (Neris et al. 2018). Previously, Assunção-Miranda et al. (2016) found that heme Co-protoporphyrin IX (CoPPIX) and Sn-protoporphyrin IX (SnPPIX) were directly inactivated both dengue virus and yellow fever virus replication in a dose-dependent manner, demonstrating that the molecular structure of porphyrin might be used to design new broad spectrum antiviral compounds with enhanced activity.
Triplet-state spin labels for highly sensitive pulsed dipolar spectroscopy
Published in Molecular Physics, 2019
M. G. Dal Farra, S. Ciuti, M. Gobbo, D. Carbonera, M. Di Valentin
The feasibility of the LaserIMD experiment under photoexcitation of an endogenous prosthetic group in protein, the low-spin ferric heme moiety, was also investigated. The Cytochrome C from Saccharomyces cerevisiae labelled with MTSSL on the free cysteine 102 was used as a paradigmatic protein. In this case, the modulation of the LaserIMD trace, which corresponds to the distance between the nitroxide spin label and the heme group, cannot be ascribed to the dipolar interaction between the radical and the triplet state produced by photoexcitation since no triplet-state signal was detected. The presence of the Fe(III) coordinated to the heme moiety complicates the photoexcitation pathways in the protein. Zn-substitution of the heme is necessary in order to populate the Zn(II) protoporphyrin IX triplet state and unambiguously prove the feasibility the triplet–nitroxide LaserIMD experiment using endogenous spin probes like heme.