(A) In the sequence alignment, a black background marks sequence identity, and the wedges show the predicted iron binding sites. (B) In the protein structure, ligands for non-heme iron are shown in yellow. The black and red residue numbers are correspond to PerR and Irr, respectively. ...
coli strain that overexpressed the genes involved in the heme b synthesis [9]. To increase the availability of succinyl-CoA, a NADPH-dependent malic enzyme (MacB) and a C4-dicarboxylic acid transporter protein (DctA) were considered for the study of the heme b production. MacB catalyzed the...
H2O2 molecules were placed outside the protein. After reaching equilib- rium, root-mean-square fluctuation followed closely the B–values of the crystal structure; however, amino acid mobility was generally larger in water and even more in H2O2. Channel permeability to the solvent was tested with...
HO-1 is widely expressed as a type II membrane protein throughout mammals, which predominantly anchors to the endoplasmic reticulum membrane with its hydrophobic carboxy-termini. In addition, the distinct subcellular localization of HO-1 has also been reported, including the caveolae, the nucleus, ...
Densitometry was done by Quantity One software to quantify HO-1 protein level (C). Relative HO-1 protein level taking root sample (R) as 100%. A HO1 B L S R B GS 31 KD C 1.6 1.4 1.2 1 0.8 0.6 0.4 2.7. Expression of TaHO1 Gene in Responses to Different Exogenous Chemicals and...
After protein separation, whole proteins were transferred onto PVDF membranes and blocked with blocking buffer (5% skim milk) for 1.5 h at room temperature (RT). After three rinses with Tris-buffered saline containing 0.1% Tween-20 (TBS-T), primary antibodies (dilution factor was 1 to 1000)...