Expression, purification, and characterization of the recombinant putative periplasmic hemin-binding protein (HutB) of Photobacterium damselae subsp. piscicida.
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.
Department of Biomolecular Science, Section of Biotechnology, University of Urbino Carlo Bo, via T. Campanella, Fano, PU, Italy. francesca.andreoni@uniurb.it
Francesca
F
Andreoni
Romina
R
Boiani
Giordano
G
Serafini
Irene
I
Bianconi
Sabrina
S
Dominici
Francesca
F
Gorini
Mauro
M
Magnani
D002352:Carrier Proteins / Q000096:biosynthesis* / Q000302:isolation & purification* / Q000378:metabolism; D015870:Gene Expression; D000081062:Heme-Binding Proteins; D006420:Hemeproteins / Q000096:biosynthesis* / Q000302:isolation & purification* / Q000378:metabolism; D019897:Periplasm; D010776:Photobacterium / Q000166:cytology*; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000302:isolation & purification* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D002352:Carrier Proteins; D000081062:Heme-Binding Proteins; D006420:Hemeproteins; D011994:Recombinant Proteins