ReviewMicrobiology and molecular biology reviews : MMBR2008
Evolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein fold.
Review in Microbiology and molecular biology reviews : MMBR, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 49 citations in OpenAlex.
- Emerging roles of pterins as signaling molecules in bacteria.Biochemical Society transactions · 2026Review
- Studying organosulfonate metabolism in southern Russia chernozem soil microbial community: ubiquity of the desulfonation pathways and possible mixotrophy in common soil heterotrophs.Archives of microbiology · 2026Article
- Article
- Control of biofilm formation by anProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Control of Biofilm Formation by anbioRxiv : the preprint server for biology · 2023Article
- A novel bacterial sulfite dehydrogenase that requires threeApplied and environmental microbiology · 2023Article
- Molybdenum and Tungsten Cofactors and the Reactions They Catalyze.Metal ions in life sciences · 2020Article
- Addressing Ligand-Based Redox in Molybdenum-Dependent Methionine Sulfoxide Reductase.Journal of the American Chemical Society · 2020Article
- Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria.Frontiers in microbiology · 2020Review
- A Two-component NADPH Oxidase (NOX)-like System in Bacteria Is Involved in the Electron Transfer Chain to the Methionine Sulfoxide Reductase MsrP.The Journal of biological chemistry · 2017Article
- Article
- Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons.Nature · 2015Article
- Pyranopterin Coordination Controls Molybdenum Electrochemistry in Escherichia coli Nitrate Reductase.The Journal of biological chemistry · 2015Article
- Article
- Oxyl and hydroxyl radical transfer in mitochondrial amidoxime reducing component-catalyzed nitrite reduction.Journal of the American Chemical Society · 2015Article
- Sulfite-oxidizing enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Review
- Electronic structure contributions to reactivity in xanthine oxidase family enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Review
- Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Review
- Molybdenum site structure of MOSC family proteins.Inorganic chemistry · 2014Article
- The mononuclear molybdenum enzymes.Chemical reviews · 2014Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
summaryThe importance of molybdoenzymes is exemplified both by the debilitating and fatal human diseases caused by their deficiency and by their persistence throughout evolution. Here, we show that the protein fold of the molybdopyranopterin-containing domain of sulfite oxidase (the SUOX fold) can be found in all three domains of life. Analyses of sequence data and protein structure comparisons (secondary structure matching) show that the SUOX fold is found in enzymes that have quite distinct macromolecular architectures comprising one or more domains and sometimes subsidiary subunits. These are summarized as follows: (i) animal SUOXs that contain an N-terminal cytochrome b(5) domain and an SUOX fold fused to a C-terminal dimerization domain; (ii) plant SUOX that contains an SUOX fold fused to a C-terminal dimerization domain; (iii) the YedY protein from Escherichia coli, which comprises only the SUOX fold; (iv) the sulfite dehydrogenase from Starkeya novella that contains the SUOX fold, a dimerization domain, and an additional c-type cytochrome subunit; and (v) the plant-type nitrate reductases, exemplified by that of Pichia angusta, that contain an N-terminal SUOX fold, a dimerization domain, a cytochrome b(5) domain, and a C-terminal NADH binding flavin adenine dinucleotide-containing domain. We used the primary sequences of the proteins containing an SUOX fold to mine 559 sequences of related proteins. A phylogeny of a nonredundant subset of these sequences was generated, and the resultant clades were categorized by sequence motif analyses in the context of the available protein structures. Based on the motif analyses, cladistics, and domain conservations, we are able to postulate a plausible pathway of SUOX fold enzyme evolution.
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