Production of functional human fetal hemoglobin in Nicotiana benthamiana for development of hemoglobin-based oxygen carriers

Kanagarajan, Selvaraju; Carlsson, Magnus; Chakane, Sandeep; Kettisen, Karin; Smeds, Emanuel; Kumar, Ranjeet; Ortenlöf, Niklas; Gram, Magnus; Åkerström, Bo; Bülow, Leif; Zhu, Lu

doi:10.1016/j.ijbiomac.2021.06.102

Cited by 2 publications

(1 citation statement)

References 61 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To further address the underlying mechanism of how T57C mutation leads to thermostability increase in clMagR, far-UV CD spectroscopy (190–260 nm) was applied to follow the unfolding and folding of proteins as a function of temperature from 25 to 95°C at 1°C intervals ( Figures 5C,D ) ( Kanagarajan et al, 2021 ; Wensien et al, 2021 ). The clMagR T57C mutant showed improved thermostability compared with clMagR WT in the temperature range we recorded ( Figures 5C,D ).…”

Section: Resultsmentioning

confidence: 99%

The rational design of iron-sulfur cluster binding site for prolonged stability in magnetoreceptor MagR

Tong

Zhou²,

Fei³

et al. 2022

Front. Mol. Biosci.

View full text Add to dashboard Cite

Iron-sulfur proteins play essential roles in a wide variety of cellular processes such as respiration, photosynthesis, nitrogen fixation and magnetoreception. The stability of iron-sulfur clusters varies significantly between anaerobic and aerobic conditions due to their intrinsic sensitivity to oxygen. Iron-sulfur proteins are well suited to various practical applications as molecular redox sensors or molecular “wires” for electron transfer. Various technologies have been developed recently using one particular iron-sulfur protein, MagR, as a magnetic tag. However, the limited protein stability and low magnetic sensitivity of MagR hindered its wide application. Here in this study, the iron-sulfur binding site of pigeon clMagR was rationally re-designed. One such mutation, T57C in pigeon MagR, showed improved iron-sulfur binding efficiency and higher iron content, as well as prolonged thermostability. Thus, clMagRT57C can serve as a prototype for further design of more stable and sensitive magnetic toolbox for magnetogenetics in the future.

show abstract

Section: Resultsmentioning

confidence: 99%