BIOC 3110 Lecture Notes - Lecture 31: Glutamate Dehydrogenase, Nitrogen Fixation, Nitrogenase

• School: University of Iowa
• Department: Biochemistry
• Course: BIOC 3110
• Professor: marcwold

Document Summary

, cells have to have amino acids that are either made or supplied by the diet. What are the two components of nitrogenase and what do they catalyze: of this complex, there is a reductase and nitrogenase, reductase- iron protein that generates high energy electrons (electrons come from ferredoxin) Structure: iron sulfur complex, allowing the high energy electron chemistry to occur: nitrogenase-converts n2 nh3 by transfer of electrons. The aminotranserases add the glutamate to a carbon skeleton. What are the steps in synthetic pathways of: aspartate: Oxaloacetate(from cac) + glutamate alphaketoglutarate + asparate. Uses cofactor plp for transaminase: alanine: Pyruvate (from glycolysis) + glutamate alphaketoglutarate + alanine. Uses cofactor plp for transaminase: serine: Addition of nh3 to alphakeotglutarate glutamate. 3pg (from glycolysis) + glutamate alphaketoglutarate + serine. Uses cofactor tetrahydrofolate to transfer one carbon groups: glycine: Same steps as serine, but once you get to serine, it is just. When the methyl is donated onto another compound, it leaves homocysteine.