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Cited by 29Metalloenzymes and iron-sulfur proteinsEnzyme Structure and FunctionMetal-Catalyzed Oxygenation Mechanisms

Adaptation to a High-Tungsten Environment: Pyrobaculum aerophilum Contains an Active Tungsten Nitrate Reductase

de Vries, Simon, Momcilovic, Milica, Strampraad, Marc J. F., Whitelegge, Julian P., Baghai, Ashkan, Schröder, Imke·2010·Biochemistry
DOI 10.1021/bi100974v
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Abstract

Nitrate reductases (Nars) belong to the DMSO reductase family of molybdoenzymes. The hyperthermophilic denitrifying archaeon Pyrobaculum aerophilum exhibits nitrate reductase (Nar) activity even at WO(4)(2-) concentrations that are inhibitory to bacterial Nars. In this report, we establish that the enzyme purified from cells grown with 4.5 μM WO(4)(2-) contains W as the metal cofactor but is otherwise identical to the Mo-Nar previously purified from P. aerophilum grown at low WO(4)(2-) concentrations. W is coordinated by a bis-molybdopterin guanine dinucleotide cofactor. The W-Nar has a 2-fold lower turnover number (633 s(-1)) but the same K(m) value for nitrate (56 μM) as the Mo-Nar. Quinol reduction and nitrate oxidation experiments monitored by EPR with both pure W-Nar and mixed W- and Mo-Nar preparations suggest a monodentate ligation by the conserved Asp241 for W(V), while Asp241 acts as a bidentate ligand for Mo(V). Redox titrations of the Mo-Nar revealed a midpoint potential of 88 mV for Mo(V/IV). The E(m) for W(V/IV) of the purified W-Nar was estimated to be -8 mV. This relatively small difference in midpoint potential is consistent with comparable enzyme activities of W- and Mo-Nars. Unlike bacterial Nars, the P. aerophilum Nar contains a unique membrane anchor, NarM, with a single heme of the o(P) type (E(m) = 126 mV). In contrast to bacterial Nars, the P. aerophilum Nar faces the cell's exterior and, hence, does not contribute to the proton motive force. Formate is used as a physiological electron donor. This is the first description of an active W-containing Nar demonstrating the unique ability of hyperthermophiles to adapt to their high-WO(4)(2-) environment.

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  • There is a natural selection of Mo in nitrate reductases.

    “indicating a natural selection of Mo in nitrate reductases.208,209”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [209]

  • The W-containing nitrate reductase from Pyrobaculum aerophilum, purified from cells grown in the presence of Mo and W, was reported to contain mostly Mo.

    “purified from cells grown in the presence of Mo and W, was reported to contain mostly Mo”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [209]

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Authors
de Vries, S., Momcilovic, M., Strampraad, M. J. F., Whitelegge, J. P., Baghai, A., & Schröder, I.
Affiliations
  • Laboratory of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands
  • Biomedical Engineering Interdepartmental Program
  • Delft University of Technology (NL)
  • Department of Chemistry and Biochemistry
  • Department of Microbiology, Immunology, and Molecular Genetics
Corresponding author
Schröder, Imke
ORCID
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2010-10-21
Volume
49
Issue
45
Pages
9911-9921
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi100974v
OpenAlex
W2316463943
Cited by
29
References
63
Citations by year
2026: 1 · 2025: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 3 · 2019: 2 · 2017: 5 · 2016: 1 · 2015: 1 · 2014: 2 · 2013: 3 · 2012: 2
FWCI
1.49
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Center for Research Resources (R21RR021913)
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords
Pyrobaculum aerophilum, hyperthermophilic archaea, denitrification, enzyme turnover number, midpoint potential, nitrate oxidation
MeSH terms
Acclimatization, Electron Spin Resonance Spectroscopy, Environment, Kinetics, Nitrite Reductases, Oxidation-Reduction, Mass Spectrometry, Tungsten, Catalytic Domain, Protein Subunits, Pyrobaculum, Nitrate Reductase

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