Abstract
Recent advances in DNA sequencing technologies have provided unprecedented access into the diversity of the microbial world. Herein we use the comparative genomic analysis of microbial genomes and environmental metagenomes coupled with structural modelling to explore the diversity of aerobic respiration in Archaea. We focus on the heme-copper oxidoreductase superfamily which is responsible for catalyzing the terminal reaction in aerobic respiration - the reduction of molecular oxygen to water. Sequence analyses demonstrate that there are at least eight heme-copper oxygen reductase families: A-, B-, C-, D-, E-, F-, G-, and H-families. Interestingly, five of these oxygen reductase families (D-, E-, F-, G-, and H-families) are currently found exclusively in Archaea. We review the structural properties of all eight families focusing on the members found within Archaea. Structural modelling coupled with sequence analysis suggests that many of the oxygen reductases identified from thermophilic Archaea have modified proton channel properties compared to the currently studied mesophilic bacterial oxygen reductases. These structural differences may be due to adaptation to the specific environments in which these enzymes function. We conclude with a brief analysis of the phylogenetic distribution and evolution of Archaeal heme-copper oxygen reductases.
| Original language | English (US) |
|---|---|
| Title of host publication | Bioenergetics |
| Subtitle of host publication | Energy Conservation and Conversion |
| Editors | Günter Schäfer, Harvey Penefsky |
| Pages | 1-31 |
| Number of pages | 31 |
| DOIs | |
| State | Published - Jun 5 2008 |
Publication series
| Name | Results and Problems in Cell Differentiation |
|---|---|
| Volume | 45 |
| ISSN (Print) | 0080-1844 |
| ISSN (Electronic) | 1861-0412 |
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ASJC Scopus subject areas
- Developmental Biology
- Cell Biology
Cite this
Diversity of the Heme-Copper superfamily in archaea : Insights from genomics and structural modeling. / Hemp, James; Gennis, Robert B.
Bioenergetics: Energy Conservation and Conversion. ed. / Günter Schäfer; Harvey Penefsky. 2008. p. 1-31 (Results and Problems in Cell Differentiation; Vol. 45).Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Diversity of the Heme-Copper superfamily in archaea
T2 - Insights from genomics and structural modeling
AU - Hemp, James
AU - Gennis, Robert B.
PY - 2008/6/5
Y1 - 2008/6/5
N2 - Recent advances in DNA sequencing technologies have provided unprecedented access into the diversity of the microbial world. Herein we use the comparative genomic analysis of microbial genomes and environmental metagenomes coupled with structural modelling to explore the diversity of aerobic respiration in Archaea. We focus on the heme-copper oxidoreductase superfamily which is responsible for catalyzing the terminal reaction in aerobic respiration - the reduction of molecular oxygen to water. Sequence analyses demonstrate that there are at least eight heme-copper oxygen reductase families: A-, B-, C-, D-, E-, F-, G-, and H-families. Interestingly, five of these oxygen reductase families (D-, E-, F-, G-, and H-families) are currently found exclusively in Archaea. We review the structural properties of all eight families focusing on the members found within Archaea. Structural modelling coupled with sequence analysis suggests that many of the oxygen reductases identified from thermophilic Archaea have modified proton channel properties compared to the currently studied mesophilic bacterial oxygen reductases. These structural differences may be due to adaptation to the specific environments in which these enzymes function. We conclude with a brief analysis of the phylogenetic distribution and evolution of Archaeal heme-copper oxygen reductases.
AB - Recent advances in DNA sequencing technologies have provided unprecedented access into the diversity of the microbial world. Herein we use the comparative genomic analysis of microbial genomes and environmental metagenomes coupled with structural modelling to explore the diversity of aerobic respiration in Archaea. We focus on the heme-copper oxidoreductase superfamily which is responsible for catalyzing the terminal reaction in aerobic respiration - the reduction of molecular oxygen to water. Sequence analyses demonstrate that there are at least eight heme-copper oxygen reductase families: A-, B-, C-, D-, E-, F-, G-, and H-families. Interestingly, five of these oxygen reductase families (D-, E-, F-, G-, and H-families) are currently found exclusively in Archaea. We review the structural properties of all eight families focusing on the members found within Archaea. Structural modelling coupled with sequence analysis suggests that many of the oxygen reductases identified from thermophilic Archaea have modified proton channel properties compared to the currently studied mesophilic bacterial oxygen reductases. These structural differences may be due to adaptation to the specific environments in which these enzymes function. We conclude with a brief analysis of the phylogenetic distribution and evolution of Archaeal heme-copper oxygen reductases.
UR - http://www.scopus.com/inward/record.url?scp=44449146602&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=44449146602&partnerID=8YFLogxK
U2 - 10.1007/400_2007_046
DO - 10.1007/400_2007_046
M3 - Chapter
C2 - 18183358
AN - SCOPUS:44449146602
SN - 9783540786214
T3 - Results and Problems in Cell Differentiation
SP - 1
EP - 31
BT - Bioenergetics
A2 - Schäfer, Günter
A2 - Penefsky, Harvey
ER -