Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.99.48 extracted from

  • Lockhart, C.L.; Conger, M.A.; Pittman, D.S.; Liptak, M.D.
    Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure (2015), J. Biol. Inorg. Chem., 20, 757-770.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
an optical spectroscopic and density functional theory characterization of azide- and cyanide-inhibited wild type and N7A IsdG. Residue Asn7 perturbs the electronic structure of azide-inhibited, but not cyanide-inhibited, IsdG. The terminal amide of Asn7 is a hydrogen bond donor to the alpha-atom of a distal ligand to heme in IsdG. The Asn7-N3 hydrogen bond influences the orientation of a distal azide ligand with respect to the heme substrate. Asn7-N3 hydrogen bond donation causes the azide ligand to rotate about an axis perpendicular to the porphyrin plane and weakens the pi-donor strength of the azide ligand Staphylococcus aureus

Inhibitors

Inhibitors Comment Organism Structure
azide
-
Staphylococcus aureus
cyanide
-
Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q8NX62
-
-
Staphylococcus aureus MW2 Q8NX62
-
-