Biochemistry of Nitrogen Fixation

摘要: Publisher Summary This chapter discusses the biochemistry of nitrogen fixation. Nitrogenase is a complex enzyme that catalyzes reduction variety substrates with concomitant hydrolysis adenosine triphosphate (ATP). It contains two easily separable, iron–sulfur proteins, one which molybdenum. These require reductant, reducible substrate, an ATP-generating system, and anaerobic environment to function. The system necessary because diphosphate inhibits nitrogenase activity. Several spectroscopic techniques are used describe proteins both in isolated forms during enzymatic include electron paramagnetic resonance spectroscopy, Mossbauer UV-visible spectrophotometry, circular dichroism, X-ray absorption edge fine structure linear electric field effects. Complex formation between protein components essential for transfer. many substrates. active substrate-reducing sites contain metal atoms, oxidized reduced catalysis.