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Article

Corynebacterium diphtheriae HmuT: dissecting the roles of conserved residues in heme pocket stabilization.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Oct 2016

Draganova Elizabeth B, Adrian Seth A, Lukat-Rodgers Gudrun S, Keutcha Cyrianne S, Schmitt Michael P, Rodgers Kenton R, Dixon Dabney W

Abstract excerpt

The heme-binding protein HmuT is part of the Corynebacterium diphtheriae heme uptake pathway and is responsible for the delivery of heme to the HmuUV ABC transporter. HmuT binds heme with a conserved His/Tyr heme axial ligation motif. Sequence alignment revealed additional conserved residues of potential importance for heme binding: R237, Y272 and M292. In this study, site-directed mutations at these three...

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PMID: 27561288
DOI: 10.1007/s00775-016-1386-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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