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The molybdoproteome of Starkeya novella– insights into the diversity and functions of molybdenum containing proteins in response to changing growth conditions

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Metallomics Vol - 5 Issue - 3

Metallomics Vol - 5 Issue - 2

The molybdoproteome of Starkeya novella– insights into the diversity and functions of molybdenum containing proteins in response to changing growth conditions

Content Provider	Royal Society of Chemistry (RSC)
Author	Nouwens, Amanda S. Kappler, Ulrike
Copyright Year	2013
Abstract	Molybdenum enzymes are known to underpin key reactions in the biological carbon, nitrogen and sulfur cycles, however, the diversity of these enzymes and the reactions they catalyze especially in bacteria is much greater than currently known. We have analysed the molybdoproteome of the soil bacterium Starkeya novella as a function of growth mode and identified a complete pathway for Mo–PPT synthesis, a Mo transporter and 18 gene loci encoding mononuclear Mo-enzymes of the Xanthine Oxidase, Sulfite Oxidase and DMSO Reductase enzyme families. This relatively high number of Mo enzymes may be a specific property of the taxonomic group (Xanthobacteraceae) to which S. novella belongs. About 70% of S. novella Mo enzymes have no characterized close relatives, and two thirds of them are expressed under the conditions analysed, which included heterotrophy, methylotrophy, chemolithotrophy and mixotrophy. Many enzymes were clearly regulated in response to either the type of carbon source present in the growth medium or the presence of thiosulfate, and two, in particular, including an uncharacterized enzyme of the XO family (Snov_3370) were highly abundant under all growth conditions tested. We also uncovered novel enzymes with links to growth in the presence of thiosulfate, such as a PaoABC-type aldehyde oxidoreductase and an uncharacterized group 1 sulfite oxidase family enzyme, although the function of these enzymes during sulfur oxidation is unclear at present. Clearly, further work is needed to uncover the significance of these enzymes for cell metabolism.
Starting Page	325
Ending Page	334
Page Count	10
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	5
Issue Number	4
Journal	Metallomics
DOI	10.1039/c2mt20230a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Xanthobacteraceae DMSO Enzyme Oxidoreductase Starkeya Aldehyde Metabolism Molybdenum Carbon Novella Sulfite Heterotroph Gene Sulfite oxidase Thiosulfate Methylotroph Nitrogen fixation Bacteria Lithotroph Sulfur DMSO reductase
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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