ESR studies of protein A of the soluble methane monooxygenase from Methylococcus capsulatus (Bath)
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Summary
The ESR spectra are consistent with a centre of the haemerythin type as opposed to an iron-sulphur cluster, and are interpreted as indicative of a binuclear Fe centre as the redox site in the protein.
- Type
- article
- Published
- 1986-09-26
- Cited by
- 89
- References
- 21
- OpenAlex
- https://openalex.org/W2004582035
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:84634086
Keywords
Methane monooxygenase, Chemistry, Dithionite, Redox, Oxidoreductase
References
- Some properties of a soluble methane mono-oxygenase from Methylococcus capsulatus strain Bath.
- Physical characterization of two-iron uteroferrin. Evidence for a spin-coupled binuclear iron cluster.
- Oxidation-reduction potentials of molybdenum, flavin and iron-sulphur centres in milk xanthine oxidase.
- Microbial gas metabolism : mechanistic, metabolic, and biotechnological aspects
- Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity.
- Purification and characterization of component A of the methane monooxygenase from Methylococcus capsulatus (Bath).
- Electron spin resonance of the iron-containing protein B2 from ribonucleotide reductase.
- The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds.
- Electron transfer reactions in the soluble methane monooxygenase of Methylococcus capsulatus (Bath).
- BINUCLEAR IRON COMPLEXES IN METHEMERYTHRIN AND AZIDOMETHEMERYTHRIN AT 2. 0-A RESOLUTION.
- Reduction of methemerythrin by dithionite ion.
- Mössbauer studies on the active Fe ... [2Fe-2S] site of putidamonooxin, its electron transport and dioxygen activation mechanism.
- Spin lattice relaxation and exchange interaction in a 2-iron, 2-sulphur protein.
- Structural chemistry of hemerythrin
- Purification of component A of the soluble methane monooxygenase of Methylococcus capsulatus (Bath) by high-pressure gel permeation chromatography.
- EPR spectroscopy of semi-methemerythrin.
- Steady-state kinetic analysis of soluble methane mono-oxygenase from Methylococcus capsulatus (Bath).
- Effects of solvent on the properties of ferredoxins.
- Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoprotein.
- Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (component C) of the methane mono-oxygenase from Methylococcus capsulatus (Bath).
Cited by
- Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and two dinuclear iron clusters.
- Spectroscopic Evidence for and Characterization of a Trinuclear Ferroxidase Center in Bacterial Ferritin from Desulfovibrio vulgaris Hildenborough
- Electron transfer and radical forming reactions of methane monooxygenase.
- Methane monooxygenase: functionalizing methane at iron and copper.
- Transfer of a quadridentate N2S2 ligand from M2+ (M=Cr, Mn, Fe, Co or Ni) to Cu2+: Unexpected reactivities of bimetallic intermediates
- Transient intermediates of the methane monooxygenase catalytic cycle.
- Oxidation of deuterated compounds by high specific activity methane monooxygenase from Methylosinus trichosporium. Mechanistic implications.
- Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction.
- Perspectives on non-heme iron protein chemistry.
- Electrochemical properties of the diiron core of uteroferrin and its anion complexes.
- Mössbauer Spectra and Crystal Structure of Dinuclear Iron(II,III) Complex [Fe2(bpmp)(ena)2](BF4)2 of a Septadentate Polypyridine Ligand (Hbpmp): An Example of Fast Electron Interexchange
- Determining the Structure of a Hydroxylase Enzyme That Catalyzes the Conversion of Methane to Methanol in Methanotrophic Bacteria
- The functionalisation of saturated hydrocarbons. Part XXI. The Fe(III)-catalyzed and the Cu(II)-catalyzed oxidation of saturated hydrocarbons by hydrogen peroxide: a comparative study
- ON THE REACTION MECHANISM OF PROPANE HYDROXYLATION WITH METHYLOSINUS TRICHOSPORIUM (OB3B)
- The selective functionalization of saturated hydrocarbons: Gif chemistry
- Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster
- EPR Studies of the Mitochondrial Alternative Oxidase
- Crystallization and preliminary X-ray analysis of the methane monooxygenase hydroxylase protein from Methylococcus capsulatus (Bath).
- Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins.
- The Leeuwenhoek Lecture 2000 The natural and unnatural history of methane-oxidizing bacteria
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