Eugene V. Koonin Nature Genetics 12, 237–239 (1996) Fig. 1 was improperly aligned. . 1996 Nature Publishing GroupKoonin, E. V. et al.Springer NatureNature GeneticsKoonin E.V. (1996) Human choroideremia protein contains a FAD-binding domain. Nature Genet. , 12 , 237–239....
In order to demonstrate where FMO interacts with FAD, four mutants for the rat liver FMO1 protein were expressed in yeast and characterized. All four mutants were immunochemically similar to the unmodified form, although the contents of FAD in all four mutants were much lower than that in the...
Ferroptosis is characterized by unchecked lipid peroxidation and disruption of the cell membrane, resulting in mortality1. Human ferroptosis suppressor protein 1 (hFSP1), which utilizes 6-OH-FAD as the primary cofactor, prevents lipid peroxidation by oxidizing NAD(P)H and reduces coenzyme Q/vitamin ...
Structure of the substrate-binding site AfGDH/LGC contains two LGC molecules, which were found in the catalytic site and at the protein surface. The electron density of the LGC bound on the surface of protein was relatively weak (Fig. 3 (f)). The bound LGC was located at inter-molecular...
We report the crystal structure of the FAD/NADPH-binding domain (FAD domain) of the biotechnologically important Bacillus megaterium flavocytochrome P450 BM3, the last domain of the enzyme to be structurally resolved. The structure was solved in both the absence and presence of the ligand NADP(+...
Glutathione reductase from human erythrocytes: amino-acid sequence of the structurally known FAD-binding domain. Glutathione reductase from human erythrocytes: amino-acid sequence of the structurally known FAD-binding domain. Eur J Biochem 1981;120(2):407-19... R Untucht-Grau,R Heinerschirmer,I ...
S2) suggested that the V492E mutation had little effect on the protein secondary structure. This was surprising, in light of the structural role of FAD in bridging the FAD-binding β-barrel and C-terminal NADPH-binding domain of the rat enzyme through hydrogen bonds and hydrophobic interactions...
However, mutations that directly evidence the function of gp91phox in FAD binding are not reported. We found an X-linked CGD patient whose neutrophils peculiarly expressed cytochrome b 558 containing heme, with a diminished amount of gp91phox protein but a relatively high level of p22phox. ...
Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry 35, 7684–7691 (1996). Article CAS Google Scholar Kemmink, J. et al. The structure in solution of the b domain of protein ...
FAD binding site is located between the protein domains and has been described in detail by Bruns & Karplus [4]. The binding of the prosthetic group to FNRs from different sources is structurally different. The crystal structures of enzymes from plastids and cyanobacteria have FAD molecule in an...