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Prospects for Exploiting Microbes and Plants for Bioremediation of Heavy Metals
Published in Maulin P. Shah, Removal of Refractory Pollutants from Wastewater Treatment Plants, 2021
Hiren K. Patel, Rishee K. Kalaria, Divyesh K. Vasava
MTs are low-molecular-mass, cysteine-rich, metal-binding proteins that are used for heavy metal detoxification by intracellular sequestration. These chelators bind to the metals and type a fancy that is transported to the vacuole. As an example Zinc (Zn+2) is transported into the vacuole by MTPs (metal tolerance proteins). MTP1 and MTP3 localize at the vacuolar membrane and are used to form the plant metallic element tolerance (Gustin et al., 2009). Within the case of Cd, AtHMA3 plays a role in its accumulation in the vacuole. For copper (Cu+2), transporters like PAA1 (HMA6) [P-type ATPase of Arabidopsis1 (heavy metal ATPase6)], PAA2 (HMA8) [P-type ATPase of Arabidopsis2 (heavy metal ATPase8)], and HMA1 (heavy metal ATPase1) are important for the transportation of copper (Cu+2) into plastocyanin within the plastid. Copper (Cu+2) may also be transported into the mitochondria once it enters the metastasis negatron transport chain. Then intracellular distribution of metals is completed by chaperons. Metal chaperones along with ATPases assist in the detoxification of heavy metals in roots (Andrés‐Colás et al., 2006).
Agri-Applications of Nano-Scale Micronutrients
Published in Ramesh Raliya, Nanoscale Engineering in Agricultural Management, 2019
Copper can exist in its monovalent (Cu+) or divalent (Cu2+) form. This micronutrient is component of various metabolic compounds, such as plastocyanin, photosystem I, cytochrome oxidase and Cu-Zn superoxide dismutase. Initial studies of the effect of copper nanofertilizer on wheat showed inhibition of seedling growth (Lee et al. 2008). However, in the leafy-green vegetable, lettuce, Cu NP exposure enhanced the root and shoot lengths (Shah and Belozerova 2009). Another study on Cicer arietinum showed enhanced seed germination rates, vegetative growth, total chlorophyll and protein contents on exposure to copper NP-carbon nanofiber (Cu-CNM) composite material that ensured the slow release of the micronutrient Cu from the CNM matrix (Ashfaq et al. 2016).
Reaction Centers as Nanoscale Photovoltaic Devices
Published in Swee Ching Tan, Photosynthetic Protein-Based Photovoltaics, 2018
PSI is one of two membrane-embedded pigment-protein photosystems found in the plants, algae, and cyanobacteria that constitute the oxygenic phototrophs. It is a solar-powered oxidoreductase, using the energy of a single photon to transfer a single electron from a water-soluble redox protein, usually plastocyanin, on one side of the photosynthetic membrane to a second water-soluble redox protein, ferredoxin, on the opposite side of the membrane. Light energy is required to power this transfer because plastocyanin is considerably more oxidizing than ferredoxin, so the membrane-spanning electron transfer takes place against an overall gradient of reduction potential. The electrons that emerge from PSI are sufficiently electronegative to be able to reduce NADP + to NADPH, a reaction carried out by a ferredoxin:NADP + oxidoreductase. This NADPH is then used to power biosynthetic reactions. In-depth reviews of the composition, structure, and mechanism of PSI are available.3,6–10,32–38
Diamond morphology CuO nanomaterial’s elastic properties, ADMET, optical, structural studies, electrical conductivity and antibacterial activities analysis
Published in Inorganic and Nano-Metal Chemistry, 2022
P. Vivek, M. Rekha, A. Suvitha, M. Kowsalya, Ananth Steephen
Copper is well known for its antimicrobial activity long ago and has been recognized by the American Environmental Protection Agency as the first metallic antimicrobial agent in 2008.[34] The waterborne hospital-acquired infections and antibiotic resistance, research on copper as an antimicrobial agent is very essential. Several research have shown the variety of copper nano particles could significantly enhance the antimicrobial activity. In enzymes, copper NPs serve as electron donor/acceptor by alternating between their redox states. The copper proteins, such as plastocyanins, azurins, will be electron carriers. Depending on coordination of copper and protein, the redox potential of copper may vary. And, the redox properties of copper NPs can cause cellular damage in the foodborne pathogens, namely E. coli and L. monocytogenic.[34]
Impact of copper treatment on phenylpropanoid biosynthesis in adventitious root culture of Althaea officinalis L.
Published in Preparative Biochemistry & Biotechnology, 2022
Yun Ji Park, Nam Su Kim, Ramaraj Sathasivam, Yong Suk Chung, Sang Un Park
For plants, copper (Cu) is an essential element when present in lesser quantities, although it exerts negative effects in excessive quantities.[8] This metal is related to numerous physiological and biochemical processes.[9] Cu is a structural constituent of a variety of regulatory proteins and involves important functions in cell wall metabolism, mitochondrial respiration, photosynthetic electron transport, oxidative stress reactions, protein synthesis, hormone signaling, and ethylene sensing. Moreover, it is inserted into electron carrier proteins, such as plastocyanin which account for approximately 50% of the Cu in the plastids.[10] Due to its ability to easily lose and recover electrons, Cu serves as a cofactor in a variety of enzymes such as amino oxidase, Cu/Zn superoxide dismutase, cytochrome c oxidase, laccase, plastocyanin, and polyphenol oxidase.[11,12]
Theoretical study on interaction of cytochrome f and plastocyanin complex by a simple coarse-grained model with molecular crowding effect
Published in Molecular Physics, 2018
Satoshi Nakagawa, Isman Kurniawan, Koichi Kodama, Muhammad Saleh Arwansyah, Kazutomo Kawaguchi, Hidemi Nagao
Plastocyanin (Pc) is a small soluble protein and one of type I copper proteins. The structure of Pc by X-ray analysis has been presented by many groups [1–4]. The active site of Pc consists of one copper ion coordinated by two histidines, one cystein in a trigonal planar structure, and variable axial ligands such as the sulfur ion of methionine. Pc has the function of the electron transfer from cytochrome f (Cytf) in cytochrome b6f complex to P700 in photosystem I. The structure of Cytf has been established by C. J. Carrell and coworkers [5]. Cytf is unique among c-type cytochromes in its fold and heme ligation and has the soluble domain in the lumen-side segment. The reduction reaction of Pc is rapid with the complex between the soluble domain in Cytf and soluble Pc. The structure of the short-lived and weak complex between Cytf and Pc has been investigated by some groups [6–9]. Crowley and coworkers [8] have discussed the structure of the Cytf-Pc complex in relation to the hydrophobic interaction. The possible structures of the Cytf-Pc complex in the electron transfer reaction have been also discussed from the viewpoint of the balance between the electrostatic and hydrophobic interactions by I. Diaz-Moreno and coworkers [9]. The interaction between PC and Cytf has been experimentally investigated by several mutations of PC to elucidate the site of the electron transfer and the docking regions of molecules in relation to the reaction rate of the reduction reaction of PC [10].