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

open access: bronzeEuropean 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 ...
Leonard E. Mortenson, Walter G. Zumft
semanticscholar   +5 more sources

Purification, metal composition and properties of molybdo-ferredoxin and azoferredoxin, two of the components of the nitrogen-fixing system of Clostridium pasteurianum

Biochimica et Biophysica Acta (BBA) - General Subjects, 1967
Abstract A procedure for the separation and purification of two components of Clostridium pasteurianum involved in N2 fixation are presented. One of the components, molybdo-ferrodoxin, was about 78% pure based on a molybdenum content of 1 atom per molecule and a mol. wt. of 100 000. At this stage of purity it contained per Mo atom 1 atom Mg, 12 atoms
J.A. Morris   +2 more
openaire   +4 more sources

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