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November 20, 2007Biochemistry

Identification of Two Heme-Binding Sites in the Cytoplasmic Heme-Trafficking Protein PhuS from Pseudomonas aeruginosa and Their Relevance to Function

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Authors

DBDarci R BlockMayo ClinicGLGudrun S. Lukat-RodgersNorth Dakota State UniversityKRKenton R. RodgersNorth Dakota State University

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Block et al. (2007) studied this question.

synapsesocial.com/papers/6a9abec044c3282f559e41a4https://doi.org/10.1021/bi701509n
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Identification of the Proximal Ligand His-20 in Heme Oxygenase (Hmu O) from Corynebacterium diphtheriae2000 · 39 citations
  2. 2Shigella dysenteriaeShuS Promotes Utilization of Heme as an Iron Source and Protects against Heme Toxicity2005 · 69 citations
  3. 3Spectroscopic Characterization of Nonnative Conformational States of Cytochrome <i>c</i>2002 · 232 citations
  4. 4The Cytoplasmic Heme-binding Protein (PhuS) from the Heme Uptake System of Pseudomonas aeruginosa Is an Intracellular Heme-trafficking Protein to the δ-Regioselective Heme Oxygenase2006 · 90 citations