Document Detail


The prokaryotic complex iron-sulfur molybdoenzyme family.
MedLine Citation:
PMID:  17964535     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Bacterial genomes encode an extensive range of respiratory enzymes that enable respiratory metabolism with a diverse group of reducing and oxidizing substrates under both aerobic and anaerobic growth conditions. An important class of enzymes that contributes to this broad diversity is the complex iron-sulfur molybdoenzyme (CISM) family. The architecture of this class comprises the following subunits. (i) A molybdo-bis(pyranopterin guanine dinucleotide) (Mo-bisPGD) cofactor-containing catalytic subunit that also contains a cubane [Fe-S] cluster (FS0). (ii) A four-cluster protein (FCP) subunit that contains 4 cubane [Fe-S] clusters (FS1-FS4). (iii) A membrane anchor protein (MAP) subunit which anchors the catalytic and FCP subunits to the cytoplasmic membrane. In this review, we define the CISM family of enzymes on the basis of emerging structural and bioinformatic data, and show that the catalytic and FCP subunit architectures appear in a wide range of bacterial redox enzymes. We evaluate evolutionary events involving genes encoding the CISM catalytic subunit that resulted in the emergence of the complex I (NADH:ubiquinone oxidoreductase) Nqo3/NuoG subunit architecture. We also trace a series of evolutionary events leading from a primordial Cys-containing peptide to the FCP architecture. Finally, many of the CISM archetypes and related enzymes rely on the tat translocon to transport fully folded monomeric or dimeric subunits across the cytoplasmic membrane. We have used genome sequence data to establish that there is a bias against the presence of soluble periplasmic molybdoenzymes in bacteria lacking an outer membrane.
Authors:
Richard A Rothery; Gregory J Workun; Joel H Weiner
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2007-09-18
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1778     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2008 Sep 
Date Detail:
Created Date:  2008-09-01     Completed Date:  2008-11-17     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1897-929     Citation Subset:  IM    
Affiliation:
Membrane Protein Research Group, Department of Biochemistry, 474 Medical Sciences Building, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Catalytic Domain / physiology
Evolution
Iron-Sulfur Proteins / chemistry*,  classification,  metabolism*
Membrane Proteins / chemistry,  metabolism
Models, Biological
Models, Molecular
Molecular Sequence Data
Molybdenum / chemistry*
Oxidation-Reduction
Periplasm / chemistry,  enzymology,  metabolism
Phylogeny
Prokaryotic Cells / chemistry,  enzymology*
Protein Subunits / chemistry,  physiology
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Iron-Sulfur Proteins; 0/Membrane Proteins; 0/Protein Subunits; 7439-98-7/Molybdenum

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