A disulphide bond-mediated hetero-dimer of a hemoprotein and a fluorescent protein exhibiting efficient energy transfer

Abstract

Hetero-dimerization of a hemoprotein and green fluorescent protein via a thiol–disulphide exchange reaction is achieved. The heterodimer has suitable cross-linking points and displays efficient energy transfer.

Programming interchangeable and reversible heterooligomeric protein self-assembly using a bifunctional ligand

“…Then, the chemical space for articially designed protein-assembled structures and functions remains limited. Alternatively, self-assembly of two protein components can be achieved through gene fusion, 18,19 disulphide bond, 20 gene fusion and covalent linkage, 21 host-guest interaction, 22 and computational design. [23][24][25][26] However, their components are not easily interchangeable unless their gene constructs or PPIs are redesigned from scratch.…”

Self-oxidation of cysteine to sulfinic acid in an engineered T67C myoglobin: structure and reactivity

“…The fluorescence spectra showed that T67C-FL Mb exhibited a very low intensity at 526 nm compared to that of the free FL at 525 nm, which suggests that an energy transfer occurred since FL was linked close to the heme group, as reported recently by Hayashi and co-workers. 29 …”

“…The fluorescence spectra showed that T67C-FL Mb exhibited a very low intensity at 526 nm compared to that of the free FL at 525 nm, which suggests that an energy transfer occurred since FL was linked close to the heme group, as reported recently by Hayashi and co-workers. 29 To provide evidence for the energy transfer, we prepared apo-T67C-FL Mb by removing the heme group. The fluorescence spectrum of apo-T67C-FL Mb showed the characteristic emission at 528 nm, with the intensity higher than that of free FL.…”