Results 1 to 10 of about 315 (98)

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, W G, Zumft, L E, Mortenson
core   +5 more sources

Evidence for the Existence of a Fully Reduced State of Molybdoferredoxin during the Functioning of Nitrogenase, and the Order of Electron Transfer from Reduced Ferredoxin

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 ...
M N, Walker, L E, Mortenson
  +6 more sources

Evidence for a Catalytic‐Centre Heterogeneity of Molybdoferredoxin from Clostridium pasteurianum [PDF]

European Journal of Biochemistry, 1973
Molybdoferredoxin, the high‐molecular‐weight component of clostridial nitrogenase has been separated into two components by gradient chromatography on DEAE‐cellulose. One component when combined with azoferredoxin, the low‐molecular‐weight component of nitrogenase, does not reduce acetylene, evolve hydrogen from dithionite or hydrolyse ATP; the other ...
W G, Zumft, L E, Mortensson
openaire   +3 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.
openaire   +4 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.
W G, Zumft, L E, Mortenson, G, Palmer
openaire   +2 more sources

Structural Insights and Mechanistic Understanding of Iron-Molybdenum Cofactor Biosynthesis by NifB in Nitrogenase Assembly Process. [PDF]

Mol Cells, 2023
Kang W.
europepmc   +1 more source

Comment on "Structural evidence for a dynamic metallocofactor during N₂ reduction by Mo-nitrogenase". [PDF]

Science, 2021
Peters JW, Einsle O, Dean DR, DeBeer S, Hoffman BM, Holland PL, Seefeldt LC.   +6 more
europepmc   +1 more source

¹³C ENDOR Characterization of the Central Carbon within the Nitrogenase Catalytic Cofactor Indicates That the CFe₆ Core Is a Stabilizing "Heart of Steel". [PDF]

J Am Chem Soc, 2022
Lukoyanov DA, Yang ZY, Pérez-González A, Raugei S, Dean DR, Seefeldt LC, Hoffman BM.   +6 more
europepmc   +1 more source

Nitrogenase Chemistry at 10 Kelvin─Phototautomerization and Recombination of CO-Inhibited α-H195Q Enzyme. [PDF]

Inorg Chem, 2022
Gee LB, Myers WK, Nack-Lehman PA, Scott AD, Yan L, George SJ, Dong W, Dapper CH, Newton WE, Cramer SP.   +9 more
europepmc   +1 more source

Proton Transfer Pathways in Nitrogenase with and without Dissociated S2B. [PDF]

Angew Chem Int Ed Engl, 2022
Jiang H, Svensson OKG, Cao L, Ryde U.
europepmc   +1 more source