| Literature DB >> 25416397 |
Larry L Barton1, Marie-Laure Fardeau, Guy D Fauque.
Abstract
Sulfur is an essential element for the synthesis of cysteine, methionine, and other organo-sulfur compounds needed by living organisms. Additionally, some prokaryotes are capable of exploiting oxidation or reduction of inorganic sulfur compounds to energize cellular growth. Several anaerobic genera of Bacteria and Archaea produce hydrogen sulfide (H2S), as a result of using sulfate (SO(4)(2 -) ), elemental sulfur (S(0)), thiosulfate (S₂O(3)(2 -)), and tetrathionate (S(4)O(6)(2 -)) as terminal electron acceptors. Some phototrophic and aerobic sulfur bacteria are capable of using electrons from oxidation of sulfide to support chemolithotrophic growth. For the most part, biosulfur reduction or oxidation requires unique enzymatic activities with metal cofactors participating in electron transfer. This review provides an examination of cytochromes, iron-sulfur proteins, and sirohemes participating in electron movement in diverse groups of sulfate-reducing, sulfur-reducing, and sulfide-oxidizing Bacteria and Archaea.Entities:
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Year: 2014 PMID: 25416397 DOI: 10.1007/978-94-017-9269-1_10
Source DB: PubMed Journal: Met Ions Life Sci ISSN: 1559-0836