Rare earth metals are essential for methanotrophic life in volcanic mudpots
Arjan Pol
Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
Search for more papers by this authorThomas R. M. Barends
Department of Biomolecular Mechanisms, Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
Search for more papers by this authorAndreas Dietl
Department of Biomolecular Mechanisms, Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
Search for more papers by this authorAhmad F. Khadem
Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
Search for more papers by this authorJelle Eygensteyn
Department of General Instruments, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
Search for more papers by this authorCorresponding Author
Mike S. M. Jetten
Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
For correspondence. E-mail [email protected]; Tel. (+31) (0) 24 365 2940; Fax (+31) (0) 24 365 2830.Search for more papers by this authorHuub J. M. Op den Camp
Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
Search for more papers by this authorArjan Pol
Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
Search for more papers by this authorThomas R. M. Barends
Department of Biomolecular Mechanisms, Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
Search for more papers by this authorAndreas Dietl
Department of Biomolecular Mechanisms, Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
Search for more papers by this authorAhmad F. Khadem
Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
Search for more papers by this authorJelle Eygensteyn
Department of General Instruments, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
Search for more papers by this authorCorresponding Author
Mike S. M. Jetten
Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
For correspondence. E-mail [email protected]; Tel. (+31) (0) 24 365 2940; Fax (+31) (0) 24 365 2830.Search for more papers by this authorHuub J. M. Op den Camp
Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands
Search for more papers by this authorSummary
Growth of Methylacidiphilum fumariolicum SolV, an extremely acidophilic methanotrophic microbe isolated from an Italian volcanic mudpot, is shown to be strictly dependent on the presence of lanthanides, a group of rare earth elements (REEs) such as lanthanum (Ln), cerium (Ce), praseodymium (Pr) and neodymium (Nd). After fractionation of the bacterial cells and crystallization of the methanol dehydrogenase (MDH), it was shown that lanthanides were essential as cofactor in a homodimeric MDH comparable with one of the MDHs of Methylobacterium extorquens AM1. We hypothesize that the lanthanides provide superior catalytic properties to pyrroloquinoline quinone (PQQ)-dependent MDH, which is a key enzyme for both methanotrophs and methylotrophs. Thus far, all isolated MxaF-type MDHs contain calcium as a catalytic cofactor. The gene encoding the MDH of strain SolV was identified to be a xoxF-ortholog, phylogenetically closely related to mxaF. Analysis of the protein structure and alignment of amino acids showed potential REE-binding motifs in XoxF enzymes of many methylotrophs, suggesting that these may also be lanthanide-dependent MDHs. Our findings will have major environmental implications as metagenome studies showed (lanthanide-containing) XoxF-type MDH is much more prominent in nature than MxaF-type enzymes.
Supporting Information
Filename | Description |
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emi12249-sup-0001-si.pdf159.4 KB | Fig. S1. Uptake preference within the series of REE (La, Ce, Pr, Nd) during growth in MPW-supplemented (4%) medium. Fig. S2. SDS-PAGE (12%) of the purified methanol dehydrogenase of strain SolV (A) and the UV-Vis spectrum of the pure enzyme (B). Fig. S3. Analytical ultracentrifugation analysis of purified MDH. Fig. S4. Effect of pH on MDH activity. Activities refer to the μM DCPIP reduced per min. Each symbol represents an individual measurement. Squares and triangles indicate measurements with and without 40 mM ammonium chloride respectively. Fig. S5. A. Kinetics of purified MDH. Symbols indicate individual rate measurements. Lines represent the curves obtained by fitting Michaelis–Menten kinetics. Obtained affinity constants (Km) are given in Table 3. B. Kinetics of purified MDH. Symbols indicate individual rate measurements. Lines represent the curves obtained by fitting Michaelis–Menten kinetics. Obtained affinity constants (Km) are given in Table 3. Table S1. Crystallographic data and model quality. |
Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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