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Nature’s Green Catalyst for Environmental Remediation, Clean Energy Production, and Sustainable Development
Published in Miguel A. Esteso, Ana Cristina Faria Ribeiro, A. K. Haghi, Chemistry and Chemical Engineering for Sustainable Development, 2020
Benny Thomas, Divya Mathew, K. S. Devaky
Dioxygenases are multicomponent enzyme systems responsible for the degradation of aromatic pollutants into nontoxic materials. On the basis of their mode of action, aromatic dioxygenases have the element of both aromatic ring hydroxylation and aromatic ring cleavage. Aromatic ring hydroxylation dioxygenases degrade the chemical compounds by the addition of two molecules of oxygen into the ring while aromatic ring cleavage dioxygenases cleave the aromatic rings of compounds.4 They have Rieske (2Fe–2S) cluster and mononuclear iron in their alpha subunit, and hence, they thought to belong to the family of Rieske nonheme iron oxygenases.15Aromatic hydrocarbon dioxygenase includes toluene dioxygenase, catechol dioxygenase, and so on. They introduce molecular oxygen into their substrate.16 They are effectual for environmental remediation owing to their enantiospecific oxygenation property of a wide range of substrates
Recent Developments in the Treatment of Petroleum Hydrocarbon and Oily Sludge from the Petroleum Industry
Published in Sunil Kumar, Zengqiang Zhang, Mukesh Kumar Awasthi, Ronghua Li, Biological Processing of Solid Waste, 2019
Surendra Sarsaiya, Sanjeev Kumar Awasthi, Archana Jain, Saket Mishra, Qi Jia, Fuxing Shu, Jiao Li, Yumin Duan, Ranjan Singh, Mukesh Kumar Awasthi, Jingshan Shi, Jishuang Chen
Various key genes to understand the anaerobic and aerobic biodegradation of hydrocarbon contaminants are alkM, alkB, alkA, LadA, nahA-M, assA1, assA2, napA, dsrAB, mcrA, amoA etc. (Li et al. 2011; Feng et al. 2011; Guan et al. 2013; Liu et al. 2016; Varjani and Upasani 2017). The primary breakdown of organic contaminants is an oxidative course of action. The peroxidases and oxygenases catalyze establishment as well as absorption of oxygen molecule. Tangential pathways for degradation convert organic contaminants systematically into metabolic intermediates like Tricarboxylic Acid (TCA) (Abbasian et al. 2015). The construction of cell biomass establishes from essential microbe’s products precursor like pyruvate, acetyl-CoA, and succinate (Das and Chandran 2011). The different useful genes used for the breakdown of petro hydrocarbon are well recognized previously (Foght 2008). The most important genes participating in microbial degradation of hydrocarbon contaminants are XylE gene: catechol dioxygenase, AlkB gene: alkane monooxygenase, and naphthalene dioxygenase similar to the gene NahAc (Meckenstock et al. 2016).
BioMolecular and Chiral Self-Assembly: Skylar Tibbits, Arthur Olson, and Autodesk Inc.
Published in Skylar Tibbits, Self-Assembly Lab, 2016
The BioMolecular Self-Assembly project, completed for the TED Global Conference in 2012, is a project undertaken in collaboration with molecular biologist Arthur Olson at the Scripps Research Institute, and Autodesk Inc. This project demonstrates molecular self- assembly through tangible and physical models. The geometry and material components are based on various molecular structures, including the tobacco plant virus, a ferritin protein assembly, and catechol dioxygenase enzyme.
A review on bio-functional models of catechol oxidase probed by less explored first row transition metals
Published in Journal of Coordination Chemistry, 2022
Rashmi Rekha Tripathy, Shuvendu Singha, Sohini Sarkar
Iron-containing metalloproteins are numerous in nature. They are known for versatile biophysical applications in living organisms such as humans, plants, animals, arthropods, mollusks and bacteria. Many of them play a significant role in oxygen binding and transport (hemoglobin, hemoerythrin, chlocruorin). Moreover, as electron carriers (rubredoxin) and as electron transfer vectors (cyctchrome) they have other contributions. Iron-containing metalloenzymes like hydrogenase and catalase can participate in many important redox processes occurring in cells, while the first one helps in reversible hydrogen uptake in different microbes, the second one catalyzes dismutation of hydrogen peroxide to water and oxygen. It helps to protect cells from oxidative damage by reactive oxygen species like peroxides [75]. Catechol dioxygenase is another example of an iron-based enzyme which can catalyze oxidation of ortho diphenols (catechols) by oxidative cleavage of a C—C bond present in the phenolic substrates followed by oxygen insertion. Its mechanism is quite different than that of catechol oxidase although both involve oxidation of catechols or catecholic substrates to the corresponding quinones.
Identification and characterization of PAH-degrading endophytes isolated from plants growing around a sludge dam
Published in International Journal of Phytoremediation, 2019
Raymond O. Anyasi, Harrison I. Atagana, Rene Sutherland
Most enzymes are involved in the metabolism of organic compounds and catechol dioxygenase is an important extradiol moiety for the breaking down of aromatic rings by bacteria (Broderick 1999; Mesarch et al.2000; Peixoto et al.2011). To carry out this test, colony PCR was performed on the bacteria isolates using the specific primers:C230F (5′-AAG AGG CAT GGG GGC GCA CCG GTT CGA-3′) andC230R (5′-TCA CCA GCA AAC ACC TCG TTG CGG TTG CC-3′),