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It enables us to describe and study the influence of both the main parallel processes: chemical reactions and diffusion of radical clusters.
Briefly, when activated by the incident radiation, NPs are responsible for the emission of electron bursts and the production of radical clusters (reactive oxygen species).
We have proposed already earlier a model describing the processes (i.e., the combined effect of cluster diffusion and chemical reactions) running in individual radical clusters that might be responsible for corresponding damages of DNA molecules (i.e., formation of DSBs).
Noticeably, the gadolinium-based nanoparticles were found located in the cytoplasm [see Fig. 2b (Stefančíková et al. 2014 ], which confirms that enhancement of cell killing is initiated in the cytoplasm (likely via the production of radical clusters).
Two parallel processes, i.e., diffusion of radicals and their chemical reactions, running in corresponding radical clusters formed during energy transfer may be represented with the help of the given model.
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Sites with a posterior probability Qk > 0.67 (to select only radical cluster-specific sites [ 50- 53]) were localized on the maize BX2-5 alignment.
Detailed UV visible, resonance Raman, and Mössbauer spectroscopic studies by Cosper et al. showed that the −140 mV potential was likely due to residual [2Fe 2S] cluster residing in the radical SAM cluster site, with the lower potential −430 mV cluster assigned to the catalytic [2Fe 2S] cluster.
Importantly, the target cysteine residues of the peptides do not ligate either auxiliary cluster, and, when bound, the cysteine to be modified is located 8.9 Å from the radical SAM cluster, 8.6 Å from cluster I, and 20.8 Å from cluster II.
Additional insight into the roles of each of the radical SAM [4Fe 4S] clusters has been provided by studies of the purified CofG and CofH proteins.
While use of dithionite as a reductant resulted in the production of nearly four dAdoH molecules per F0, use of the physiological reductant flavodoxin/flavodoxin reductase resulted in just over two dAdoH molecules per F0, suggesting that two SAM molecules are required and cleaved during F0 synthesis, presumably one at each of the radical SAM clusters in the enzyme.
This electron added to the auxiliary [4Fe 4S] cluster could then be transferred back to the radical SAM cluster, regenerating the enzyme for catalysis.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com