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Engineering heme binding sites in monomeric rop

Content Provider	Springer Nature Link
Author	Di Nardo, Giovanna Di Venere, Almerinda Mei, Giampiero Sadeghi, Sheila J. Wilson, Jon R. Gilardi, Gianfranco
Copyright Year	2009
Abstract	Heme ligands were introduced in the hydrophobic core of an engineered monomeric ColE1 repressor of primer (rop-S55) in two different layers of the heptad repeat. Mutants rop-L63M/F121H (layer 1) and rop-L56H/L113H (layer 3) were found to bind heme with a K D of 1.1 ± 0.2 and 0.47 ± 0.07 μM, respectively. The unfolding of heme-bound and heme-free mutants, in the presence of guanidinium hydrochloride, was monitored by both circular dichroism and fluorescence spectroscopy. For the heme-bound rop mutants, the total free energy change was 0.5 kcal/mol higher in the layer 3 mutant compared with that in the layer1 mutant. Heme binding also stabilized these mutants by increasing the $$ Δ G_{\text{obs}}^{{{\text{H}}_{ 2} {\text{O}}}}, $$ by 1.4 and 1.8 kcal/mol in rop-L63M/F121H and rop-L56H/L113H, respectively. The reduction potentials measured by spectroelectrochemical titrations were calculated to be −154 ± 2 mV for rop-56H/113H and −87.5 ± 1.2 mV for rop-L63M/F121H. The mutant designed to bind heme in a more buried environment (layer 3) showed tighter heme binding, a higher stability, and a different reduction potential compared with the mutant designed to bind heme in layer 1.
Starting Page	497
Ending Page	505
Page Count	9
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	14
Issue Number	4
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2009-01-17
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Heme Four-helix bundle Rational design Rop Redox potential Biochemistry Microbiology
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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