Literature DB >> 23595676

Heme uptake and metabolism in bacteria.

David R Benson1, Mario Rivera.   

Abstract

All but a few bacterial species have an absolute need for heme, and most are able to synthesize it via a pathway that is highly conserved among all life domains. Because heme is a rich source for iron, many pathogenic bacteria have also evolved processes for sequestering heme from their hosts. The heme biosynthesis pathways are well understood at the genetic and structural biology levels. In comparison, much less is known about the heme acquisition, trafficking, and degradation processes in bacteria. Gram-positive and Gram-negative bacteria have evolved similar strategies but different tactics for importing and degrading heme, likely as a consequence of their different cellular architectures. The differences are manifested in distinct structures for molecules that perform similar functions. Consequently, the aim of this chapter is to provide an overview of the structural biology of proteins and protein-protein interactions that enable Gram-positive and Gram-negative bacteria to sequester heme from the extracellular milieu, import it to the cytosol, and degrade it to mine iron.

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Year:  2013        PMID: 23595676     DOI: 10.1007/978-94-007-5561-1_9

Source DB:  PubMed          Journal:  Met Ions Life Sci        ISSN: 1559-0836


  22 in total

1.  Iminoguanidines as Allosteric Inhibitors of the Iron-Regulated Heme Oxygenase (HemO) of Pseudomonas aeruginosa.

Authors:  Geoffrey A Heinzl; Weiliang Huang; Wenbo Yu; Bennett J Giardina; Yue Zhou; Alexander D MacKerell; Angela Wilks; Fengtian Xue
Journal:  J Med Chem       Date:  2016-07-11       Impact factor: 7.446

2.  Inhibiting the BfrB:Bfd interaction in Pseudomonas aeruginosa causes irreversible iron accumulation in bacterioferritin and iron deficiency in the bacterial cytosol.

Authors:  Kate Eshelman; Huili Yao; Achala N D Punchi Hewage; Jacqueline J Deay; Josephine R Chandler; Mario Rivera
Journal:  Metallomics       Date:  2017-06-21       Impact factor: 4.526

3.  Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.

Authors:  Elizabeth B Draganova; Neval Akbas; Seth A Adrian; Gudrun S Lukat-Rodgers; Daniel P Collins; John H Dawson; Courtni E Allen; Michael P Schmitt; Kenton R Rodgers; Dabney W Dixon
Journal:  Biochemistry       Date:  2015-10-26       Impact factor: 3.162

4.  Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.

Authors:  Rizvan C Uluisik; Neval Akbas; Gudrun S Lukat-Rodgers; Seth A Adrian; Courtni E Allen; Michael P Schmitt; Kenton R Rodgers; Dabney W Dixon
Journal:  J Inorg Biochem       Date:  2016-11-23       Impact factor: 4.155

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

Authors:  Elizabeth B Draganova; Seth A Adrian; Gudrun S Lukat-Rodgers; Cyrianne S Keutcha; Michael P Schmitt; Kenton R Rodgers; Dabney W Dixon
Journal:  J Biol Inorg Chem       Date:  2016-08-25       Impact factor: 3.358

6.  Heme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability.

Authors:  Neval Akbas; Elizabeth B Draganova; Darci R Block; Brian R Sook; Yau Fong Chan; Joy Zhuo; Zehava Eichenbaum; Kenton R Rodgers; Dabney W Dixon
Journal:  J Inorg Biochem       Date:  2015-11-14       Impact factor: 4.155

7.  The Detection of Hemin-Binding Proteins in Riemerella anatipestifer CH-1.

Authors:  Hebin Liao; Mafeng Liu; Xingjun Cheng; Dekang Zhu; Mingshu Wang; Renyong Jia; Shun Chen; Kunfeng Sun; Qiao Yang; Francis Biville; Anchun Cheng
Journal:  Curr Microbiol       Date:  2015-11-06       Impact factor: 2.188

8.  The hemophore HasA from Yersinia pestis (HasAyp) coordinates hemin with a single residue, Tyr75, and with minimal conformational change.

Authors:  Ritesh Kumar; Scott Lovell; Hirotoshi Matsumura; Kevin P Battaile; Pierre Moënne-Loccoz; Mario Rivera
Journal:  Biochemistry       Date:  2013-04-11       Impact factor: 3.162

9.  Replacing Arginine 33 for Alanine in the Hemophore HasA from Pseudomonas aeruginosa Causes Closure of the H32 Loop in the Apo-Protein.

Authors:  Ritesh Kumar; Yifei Qi; Hirotoshi Matsumura; Scott Lovell; Huili Yao; Kevin P Battaile; Wonpil Im; Pierre Moënne-Loccoz; Mario Rivera
Journal:  Biochemistry       Date:  2016-04-28       Impact factor: 3.162

10.  Lipocalin Blc is a potential heme-binding protein.

Authors:  Nina G Bozhanova; M Wade Calcutt; William N Beavers; Benjamin P Brown; Eric P Skaar; Jens Meiler
Journal:  FEBS Lett       Date:  2020-12-03       Impact factor: 4.124

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