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- Hemoproteins in dissimilatory sulfate- and sulfur-reducing prokaryotes. doi link

Auteur(s): Fauque G., Barton Larry

(Article) Publié: Advances In Microbial Physiology, vol. 60 p.1-90 (2012)


Ref HAL: hal-00752297_v1
PMID 22633058
DOI: 10.1016/B978-0-12-398264-3.00001-2
Exporter : BibTex | endNote
Résumé:

Dissimilatory sulfate and sulfur reduction evolved billions of years ago and while the bacteria and archaea that use this unique metabolism employ a variety of electron donors, H(2) is most commonly used as the energy source. These prokaryotes use multiheme c-type proteins to shuttle electrons from electron donors, and electron transport complexes presumed to contain b-type hemoproteins contribute to proton charging of the membrane. Numerous sulfate and sulfur reducers use an alternate pathway for heme synthesis and, frequently, uniquely specific axial ligands are used to secure c-type heme to the protein. This review presents some of the types and functional activities of hemoproteins involved in these two dissimilatory reduction pathways.