Related Experiment Video
Updated: Jun 23, 2026
Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Expression, purification, and characterization of the recombinant putative periplasmic hemin-binding protein (HutB)
Francesca Andreoni1, Romina Boiani, Giordano Serafini
1Department of Biomolecular Science, Section of Biotechnology, University of Urbino Carlo Bo, via T. Campanella, Fano, PU, Italy. francesca.andreoni@uniurb.it
Abstract:
HutB, the periplasmic hemin binding protein of Photobacterium damselae subsp. piscicida, was produced as a recombinant protein. UV-Vis spectrophotometrical analysis showed absorption spectral changes in hemin upon mixing it with the recombinant protein, indicating complex formation. Spectrophotometric titration of HutB with hemin showed saturation at a heme/HutB ratio of 1:1 and a binding affinity (K(d)) of 10 microM.
