Results 1 to 10 of about 91 (51)
Structure of the Molybdoferredoxin Complex from Clostridium pasteurianum and Isolation of Its Subunits [PDF]
Journal of Bacteriology, 1973 Highly purified molybdoferredoxin, with a specific activity of 2.6 μmoles of acetylene reduced per min per mg of protein, was obtained from Clostridium pasteurianum . The protein at concentrations above 5 mg/ml exists in solution as a tetrameric complex with two subunits each of about 60,000 and 50,000 daltons.
T. C. Huang +2 more
core +8 more sources
Molecular weight and subunit structure of molybdoferredoxin from Clostridium pasteurianum W5
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971 Abstract 1. 1. Molybdoferredoxin, a component of the nitrogenase system of Clostridium pasteurianum W5, has a molecular weight of between 160 000 to 190 000 as estimated by gel filtration. 2. 2. Sodium dodecyl sulfate-treated molybdoferredoxin gives two bands on electrophoresis, one of which has a molecular weight of 59 500 ± 1940 and the ...
Nakos, G., Mortenson, L.
core +7 more sources
Electron paramagnetic resonance studies on nitrogenase [PDF]
Archives of Biochemistry and Biophysics, 1972 Abstract Both molybdoferredoxin and azoferredoxin exhibit EPR signals. Reduced azoferredoxin has a g = 1.94 type signal characteristic of nonheme iron proteins. Reduced molybdoferredoxin has EPR signals with g-values of 2.01, 3.78 and 4.27. This resonance appears to be due to an antiferromagnetically coupled system of iron atoms with an effective ...
Jagir S. Multani +9 more
core +6 more sources
Journal of Biological Chemistry, 1974 Abstract Molybdoferredoxin from Clostridium pasteurianum W5 was studied under conditions where the nitrogenase system was turning over and molybdoferredoxin was known to be ∼90% in the EPR-silent state. Optical spectroscopy showed that the EPR-silent molybdoferredoxin species thus formed was not the same as the EPR-silent species formed by dye ...
Margaret N. Walker, Leonard E. Mortenson
semanticscholar +5 more sources
Electron‐Paramagnetic‐Resonance Studies on Nitrogenase [PDF]
European Journal of Biochemistry, 1974 The oxidation‐reduction properties of azoferredoxin, molybdoferredoxin, and the inactive species of molybdoferredoxin, all iron‐sulfur proteins purified from Clostridium pasteurianum, were studied by potentiometry combined with electron paramagnetic resonance spectroscopy at low temperature.
Leonard E. Mortenson +2 more
openaire +4 more sources
Archaea, bacteria and termite, nitrogen fixation and sustainable plants production [PDF]
, 2021 Certain bacteria and archaea are responsible for biological nitrogen fixation. Metabolic pathways usually are common between archaea and bacteria. Diazotrophs are categorized into two main groups namely: root-nodule bacteria and plant growth-promoting ...
CHENG, Qi +2 more
core +2 more sources
Electron paramagnetic resonance studies on nitrogenase. II. Interaction of adenosine 5'-triphosphate with azoferredoxin [PDF]
, 1973 The interaction of ATP with both iron-sulfur proteins of nitrogenase from Clostridium pasteurianum, azoferredoxin and molybdoferredoxin, has been studied by low-temperature EPR spectroscopy.
Mortenson, Leonard E. +2 more
core +1 more source
Electron paramagnetic resonance studies on nitrogenase. III. Function of magnesium adenosine 5'-triphosphate and adenosine 5'-diphosphate in catalysis by nitrogenase [PDF]
, 1973 The electron paramagnetic resonance spectra of azoferredoxin and molybdoferredoxin, components of the nitrogenase of Clostridium pasteurianum, disappear when the proteins are oxidized by certain dyes.
Mortenson, Leonard E. +2 more
core +1 more source
On the structure and function of nitrogenase from W5 [PDF]
, 1972 Molybdoferredoxin from W5 was fractionated into MoFd with two atoms of molybdenum per 220,000 daltons and a specific activity of 2.6 [mu]moles C2H2 reduced/min/mg protein and into a catalytically inactive species with an identical protein moiety but an ...
Cretney, Walter C. +4 more
core +1 more source
Nitrogen fixation in eukaryotes – New models for symbiosis [PDF]
, 2007 BACKGROUND: Nitrogen, a component of many bio-molecules, is essential for growth and development of all organisms. Most nitrogen exists in the atmosphere, and utilisation of this source is important as a means of avoiding nitrogen starvation.
Kneip, Christoph +3 more
core +3 more sources