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TitleGrowth of complete ammonia oxidizers on guanidine.
Journal, issue, pagesNature, Vol. 633, Issue 8030, Page 646-653, Year 2024
Publish dateAug 14, 2024
AuthorsMarton Palatinszky / Craig W Herbold / Christopher J Sedlacek / Dominic Pühringer / Katharina Kitzinger / Andrew T Giguere / Kenneth Wasmund / Per H Nielsen / Morten K D Dueholm / Nico Jehmlich / Richard Gruseck / Anton Legin / Julius Kostan / Nesrete Krasnici / Claudia Schreiner / Johanna Palmetzhofer / Thilo Hofmann / Michael Zumstein / Kristina Djinović-Carugo / Holger Daims / Michael Wagner /
PubMed AbstractGuanidine is a chemically stable nitrogen compound that is excreted in human urine and is widely used in manufacturing of plastics, as a flame retardant and as a component of propellants, and is well ...Guanidine is a chemically stable nitrogen compound that is excreted in human urine and is widely used in manufacturing of plastics, as a flame retardant and as a component of propellants, and is well known as a protein denaturant in biochemistry. Guanidine occurs widely in nature and is used by several microorganisms as a nitrogen source, but microorganisms growing on guanidine as the only substrate have not yet been identified. Here we show that the complete ammonia oxidizer (comammox) Nitrospira inopinata and probably most other comammox microorganisms can grow on guanidine as the sole source of energy, reductant and nitrogen. Proteomics, enzyme kinetics and the crystal structure of a N. inopinata guanidinase homologue demonstrated that it is a bona fide guanidinase. Incubation experiments with comammox-containing agricultural soil and wastewater treatment plant microbiomes suggested that guanidine serves as substrate for nitrification in the environment. The identification of guanidine as a growth substrate for comammox shows an unexpected niche of these globally important nitrifiers and offers opportunities for their isolation.
External linksNature / PubMed:39143220 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.58 - 3.1 Å
Structure data

EMDB-56607: CryoEM structure of guanidinase from Nitrospira inopinata
Method: EM (single particle) / Resolution: 3.1 Å

PDB-9fek:
Crystal structure of guanidinase from Nitrospira inopinata
Method: X-RAY DIFFRACTION / Resolution: 1.58 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-MN:
Unknown entry

ChemComp-NI:
NICKEL (II) ION

ChemComp-HOH:
WATER

Source
  • candidatus nitrospira inopinata (bacteria)
KeywordsMETAL BINDING PROTEIN / comammox / guanidine / guanidinase / complete ammonia oxidizer

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