An Overview of the Biochemical and Molecular Aspects of Microbial Oxidation of Inorganic Sulfur Compounds

2008 ◽  
Vol 36 (10-11) ◽  
pp. 823-829 ◽  
Author(s):  
Bidyut R. Mohapatra ◽  
W. Douglas Gould ◽  
Orlando Dinardo ◽  
David W. Koren
1999 ◽  
Vol 45 (2) ◽  
pp. 97-105 ◽  
Author(s):  
Isamu Suzuki

Microbial oxidation of inorganic sulfur compounds is governed by both chemical and enzymatic reactions. It is therefore essential to understand reactions possible in chemistry when we consider enzymatic reactions. Various oxidation states of sulfur atoms in inorganic sulfur compounds and chemical oxidation reactions as well as nucleophilic cleavage of sulfur-sulfur bonds are discussed. The scheme of enzymatic oxidation of sulfur compounds with S2-→> S0→> SO32-→> SO42-as the main oxidation pathway is discussed with thiosulfate and polythionates leading into the main pathway for complete oxidation to sulfate. Enzymatic reactions are related to chemical reactions and the use of inhibitors for S0→> SO32-and SO32-→> SO42-is discussed for analyzing and establishing reaction stoichiometries. The proposed pathway is supported by a variety of evidence in many different microorganisms including some genetic evidence if the oxidation steps include all the systems irrespective of oxidizing agents (O2, Fe3+, cytochromes etc.).Key words: sulfur, oxidation, chemical, enzymatic, reactions.


2009 ◽  
Vol 75 (16) ◽  
pp. 5209-5217 ◽  
Author(s):  
Justin L. Burns ◽  
Thomas J. DiChristina

ABSTRACT Shewanella oneidensis MR-1, a facultatively anaerobic gammaproteobacterium, respires a variety of anaerobic terminal electron acceptors, including the inorganic sulfur compounds sulfite (SO3 2−), thiosulfate (S2O3 2−), tetrathionate (S4O6 2−), and elemental sulfur (S0). The molecular mechanism of anaerobic respiration of inorganic sulfur compounds by S. oneidensis, however, is poorly understood. In the present study, we identified a three-gene cluster in the S. oneidensis genome whose translated products displayed 59 to 73% amino acid similarity to the products of phsABC, a gene cluster required for S0 and S2O3 2− respiration by Salmonella enterica serovar Typhimurium LT2. Homologs of phsA (annotated as psrA) were identified in the genomes of Shewanella strains that reduce S0 and S2O3 2− yet were missing from the genomes of Shewanella strains unable to reduce these electron acceptors. A new suicide vector was constructed and used to generate a markerless, in-frame deletion of psrA, the gene encoding the putative thiosulfate reductase. The psrA deletion mutant (PSRA1) retained expression of downstream genes psrB and psrC but was unable to respire S0 or S2O3 2− as the terminal electron acceptor. Based on these results, we postulate that PsrA functions as the main subunit of the S. oneidensis S2O3 2− terminal reductase whose end products (sulfide [HS−] or SO3 2−) participate in an intraspecies sulfur cycle that drives S0 respiration.


Polyhedron ◽  
1985 ◽  
Vol 4 (5) ◽  
pp. 775-781 ◽  
Author(s):  
Mihály T. Beck ◽  
George B. Kauffman

Sign in / Sign up

Export Citation Format

Share Document