Azotobacter vinelandii nitrogenase“Kinetics of nif gene expression and insights into the roles of FdxN and NifQ in FeMo-co biosynthesis”

  1. Jiménez Vicente, Emilio
Zuzendaria:
  1. Luis M. Rubio Herrero Zuzendaria

Defentsa unibertsitatea: Universidad Politécnica de Madrid

Fecha de defensa: 2014(e)ko iraila-(a)k 22

Epaimahaia:
  1. Juan Imperial Ródenas Presidentea
  2. José Manuel Palacios Alberti Idazkaria
  3. Abraham Esteve Núñez Kidea
  4. Enrique Flores García Kidea
  5. Antonia Herrero Moreno Kidea

Mota: Tesia

Laburpena

The Molybdenum-nitrogenase is responsible for most biological nitrogen fixation activity (BNF) in the biosphere. Due to its great agronomical importance, it has been the subject of profound genetic and biochemical studies. The Mo nitrogenase carries at its active site a unique iron-molybdenum cofactor (FeMoco) that consists of an inorganic 7 Fe, 1 Mo, 1 C, 9 S core coordinated to the organic acid homocitrate. Biosynthesis of FeMo-co occurs outside nitrogenase through a complex and highly regulated pathway involving proteins acting as molecular scaffolds, metallocluster carriers or enzymes that provide substrates in appropriate chemical forms. Specific expression regulatory factors tightly control the accumulation levels of all these other components. Insertion of FeMo-co into a P-cluster containing apo-NifDK polypeptide results in nitrogenase reconstitution. Investigation of FeMo-co biosynthesis has uncovered new radical chemistry reactions and new roles for Fe-S clusters in biology.