Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase.
This review focuses on recent developments elucidating the mechanism of the Mo-dependent nitrogenase. This enzyme, responsible for the majority of biological nitrogen fixation, is composed of two component proteins called the MoFe protein and the Fe protein. Recent progress in understanding the mechanism of this enzyme has focused on elucidating the structures of the active site metal clusters and of the proteins, understanding substrate interactions with the active site, defining the flow of electron transfer between the metal clusters, and defining the various roles of MgATP hydrolysis.
Igarashi
Robert Y
RY
Department of Chemistry and Biochemistry, Utah State University, Logan, UT 84322, USA.
Seefeldt
Lance C
LC
D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D004579:Electron Transport; D008982:Molybdenum / Q000737:chemistry / Q000378:metabolism*; D008983:Molybdoferredoxin / Q000737:chemistry / Q000378:metabolism; D009586:Nitrogen Fixation; D009591:Nitrogenase / Q000737:chemistry / Q000378:metabolism*; D019159:Nonheme Iron Proteins / Q000737:chemistry / Q000378:metabolism; D009711:Nucleotides / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
D008983:Molybdoferredoxin; D019159:Nonheme Iron Proteins; D009711:Nucleotides; D008982:Molybdenum; D000255:Adenosine Triphosphate; D009591:Nitrogenase