Ontology highlight
ABSTRACT:
SUBMITTER: Draganova EB
PROVIDER: S-EPMC4943319 | biostudies-literature | 2015 Nov
REPOSITORIES: biostudies-literature
Draganova Elizabeth B EB Akbas Neval N Adrian Seth A SA Lukat-Rodgers Gudrun S GS Collins Daniel P DP Dawson John H JH Allen Courtni E CE Schmitt Michael P MP Rodgers Kenton R KR Dixon Dabney W DW
Biochemistry 20151026 43
The heme uptake pathway (hmu) of Corynebacterium diphtheriae utilizes multiple proteins to bind and transport heme into the cell. One of these proteins, HmuT, delivers heme to the ABC transporter HmuUV. In this study, the axial ligation of the heme in ferric HmuT is probed by examination of wild-type (WT) HmuT and a series of conserved heme pocket residue mutants, H136A, Y235A, and M292A. Characterization by UV-visible, resonance Raman, and magnetic circular dichroism spectroscopies indicates th ...[more]