The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states

No abstract is available for this paper.

• Publication year

  2001

• Venue

  JBIC Journal of Biological Inorganic Chemistry

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1007/s007750100270PMID 11862546
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Theoretical modeling of putative Ni(III)--F(430) intermediates of methylcoenzyme M reductase.

  2001cited by this paper
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• Phylogenetic analysis of 18 thermophilic Methanobacterium isolates supports the proposals to create a new genus, Methanothermobacter gen. nov., and to reclassify several isolates in three species, Methanothermobacter thermautotrophicus comb. nov., Methanothermobacter wolfeii comb. nov., and Methanot

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• Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation.

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• New perspectives on anaerobic methane oxidation.

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• Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide.

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• Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture.

  1998cited by this paper
• Identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium.

  1998cited by this paper
• Crystallization and preliminary X-ray diffraction studies of methyl-coenzyme M reductase from methanobacterium thermoautotrophicum.

  1997cited by this paper
• Purified methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the nickel(I) oxidation state by titanium(III) citrate.

  1997cited by this paper
• Changes in the electronic structure around Ni in oxidized and reduced selenium-containing hydrogenases from Methanococcus voltae.

  1997cited by this paper
• Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.

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• Interactions of 77Se and 13CO with Nickel in the Active Site of Active F420-nonreducing Hydrogenase from Methanococcus voltae *

  1996cited by this paper
• Properties of the two isoenzymes of methyl-coenzyme M reductase in Methanobacterium thermoautotrophicum.

  1993cited by this paper
• Substrate-analogue-induced changes in the nickel-EPR spectrum of active methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum.

  1992cited by this paper
• Differential expression of the two methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum as determined immunochemically via isoenzyme-specific antisera.

  1992cited by this paper
• Methyl‐coenzyme M reductase preparations with high specific activity from H2‐preincubated cells of Methanobacterium thermoautotrophicum

  1991cited by this paper
• Effect of 17O2 and 13CO on EPR spectra of nickel in hydrogenase from Chromatium vinosum.

  1990cited by this paper
• Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H.

  1990cited by this paper
• The final step in methane formation. Investigations with highly purified methyl-CoM reductase (component C) from Methanobacterium thermoautotrophicum (strain Marburg).

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• New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria.

  1982cited by this paper
• Preparation of coenzyme M analogues and their activity in the methyl coenzyme M reductase system of Methanobacterium thermoautotrophicum.

  1978cited by this paper
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

  1976cited by this paper

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• My Lifelong Passion for Biochemistry and Anaerobic Microorganisms.

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  2013cites this paper
• In vivo activation of methyl-coenzyme M reductase by carbon monoxide

  2013cites this paper
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  2011cites this paper
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  2010cites this paper
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  2010cites this paper
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  2010cites this paper
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  2010cites this paper
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  2009cites this paper
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  2008cites this paper
• Probing the reaction mechanism of methyl coenzyme M reductase

  2008influential citation
• The strength of EPR and ENDOR techniques in revealing structure-function relationships in metalloproteins.

  2007cites this paper
• Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy

  2007cites this paper
• Spectroscopic and computational studies of reduction of the metal versus the tetrapyrrole ring of coenzyme F430 from methyl-coenzyme M reductase.

  2006cites this paper
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• Biological chemistry of naturally occurring thiols of microbial and marine origin.

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• Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B

  2005cites this paper
• References

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  2005cites this paper
• Spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase: a pulse EPR study.

  2005cites this paper
• Spectroscopic investigation of the nickel-containing porphinoid cofactor F430. Comparison of the free cofactor in the +1, +2 and +3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms

  2004cites this paper
• Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues

  2004cites this paper
• Characterization of the MCRred2 form of methyl-coenzyme M reductase: a pulse EPR and ENDOR study

  2003cites this paper
• Nickel uptake and utilization by microorganisms.

  2003cites this paper
• Rapid ligand exchange in the MCRred1 form of methyl-coenzyme M reductase.

  2003cites this paper
• Coenzyme B induced coordination of coenzyme M via its thiol group to Ni(I) of F430 in active methyl-coenzyme M reductase.

  2003cites this paper
• Direct determination of the number of electrons needed to reduce coenzyme F430 pentamethyl ester to the Ni(I) species exhibiting the electron paramagnetic resonance and ultraviolet-visible spectra characteristic for the MCR(red1) state of methyl-coenzyme M reductase.

  2003cites this paper
• 28 Bioinorganic chemistry

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• 67 – Biochemistry of Methyl-CoM Reductase and Coenzyme F430

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• Review: Biological methylation of less-studied elements

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• Structure and function of enzymes involved in the methanogenic pathway utilizing carbon dioxide and molecular hydrogen.

  2002cites this paper
• Coordination and geometry of the nickel atom in active methyl-coenzyme M reductase from Methanothermobacter marburgensis as detected by X-ray absorption spectroscopy

  2002cites this paper
• The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2

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• Digital Commons @ Trinity Digital Commons @ Trinity

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• Methane and ethane production rates by methyl-coenzyme 1 M reductase in cell extracts from different methanogens 2

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