Mechanical coupling in the nitrogenase complex

• Published in: PLoS computational biology Vol. 17; no. 3; p. e1008719
• Main Authors: Huang, Qi, Tokmina-Lukaszewska, Monika, Johnson, Lewis E, Kallas, Hayden, Ginovska, Bojana, Peters, John W, Seefeldt, Lance C, Bothner, Brian, Raugei, Simone
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 04.03.2021; Public Library of Science (PLoS)
• Subjects: Adenosine; Adenosine diphosphate; Adenosine triphosphate; Allosteric properties; allosteric regulation; Analysis; ATP; ATP hydrolysis; BASIC BIOLOGICAL SCIENCES; Binding sites; Biology and Life Sciences; Clusters; Communication; Coordination compounds; Coupling; covariance; Crystal structure; Crystals; deuterium; Electron transfer; Electron transport; geodesics; Graph theory; Hydrolysis; Identification and classification; Inspection; Iron; Mechanical properties; Methods; MoFe protein; Molybdenum; Nitrogen; Nitrogenase; Nucleotides; Osmosis; Osmotic pressure; Physical Sciences; Proteins; Residues; Rigid structures; Signal transduction; Structure; United States

The enzyme nitrogenase reduces dinitrogen to ammonia utilizing electrons, protons, and energy obtained from the hydrolysis of ATP. Mo-dependent nitrogenase is a symmetric dimer, with each half comprising an ATP-dependent reductase, termed the Fe Protein, and a catalytic protein, known as the MoFe pr...