Open AccessThe modular respiratory complexes involved in hydrogen and sulfur metabolism by heterotrophic hyperthermophilic archaea and their evolutionary implications
Author(s) -
Schut Gerrit J.,
Boyd Eric S.,
Peters John W.,
Adams Michael W.W.
Publication year - 2013
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1111/j.1574-6976.2012.00346.x
Subject(s) - hydrogenase , ferredoxin , archaea , pyrococcus furiosus , biology , biochemistry , cofactor , oxidoreductase , chloroflexi (class) , protein subunit , nadh dehydrogenase , bioenergetics , enzyme , gene , proteobacteria , 16s ribosomal rna , mitochondrion
Hydrogen production is a vital metabolic process for many anaerobic organisms, and the enzyme responsible, hydrogenase, has been studied since the 1930s. A novel subfamily with unique properties was recently recognized, represented by the 14‐subunit membrane‐bound [ NiFe ] hydrogenase from the archaeon P yrococcus furiosus . This so‐called energy‐converting hydrogenase links the thermodynamically favorable oxidation of ferredoxin with the formation of hydrogen and conserves energy in the form of an ion gradient. It is therefore a simple respiratory system within a single complex. This hydrogenase shows a modular composition represented by a Na + /H + antiporter domain ( M rp) and a [ NiFe ] hydrogenase domain (Mbh). An analysis of the large number of microbial genome sequences available shows that homologs of Mbh and Mrp tend to be clustered within the genomes of a limited number of archaeal and bacterial species. In several instances, additional genes are associated with the Mbh and Mrp gene clusters that encode proteins that catalyze the oxidation of formate, CO or NAD (P)H. The M bh complex also shows extensive homology to a number of subunits within the NADH quinone oxidoreductase or complex I family. The respiratory‐type membrane‐bound hydrogenase complex appears to be closely related to the common ancestor of complex I and [ NiFe ] hydrogenases in general.