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Why do nitrogenases waste electrons by evolving dihydrogen?
Author(s) -
Ogo Seiji,
Kure Bunsho,
Nakai Hidetaka,
Watanabe Yoshihito,
Fukuzumi Shunichi
Publication year - 2004
Publication title -
applied organometallic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.53
H-Index - 71
eISSN - 1099-0739
pISSN - 0268-2605
DOI - 10.1002/aoc.744
Subject(s) - chemistry , heterolysis , nitrogenase , catalysis , electron , ammonia , ion , hydrogen , liquid ammonia , nitrate , photochemistry , nitrogen , inorganic chemistry , medicinal chemistry , organic chemistry , nitrogen fixation , physics , quantum mechanics
In nature, nitrogen is commonly fixed as the most reduced form, ammonia (NH 3 ) and as the most oxidized form, i.e. nitrate ion (NO 3 − ). Nitrogenases catalyze the reduction of N 2 into NH 3 by using protons and electrons with evolution of H 2 . However, the reason why the enzymes waste electrons by evolving H 2 has yet to be clarified. We have previously reported ( J. Am. Chem. Soc. 2002; 124: 597) pH‐dependent heterolytic cleavage of H 2 and subsequent reduction of NO 3 − with evolution of H 2 by iridium complexes in water. We propose herein a catalytic mechanism of nitrogenases, which can account for evolution of H 2 in the reduction of N 2 to NH 3 in relation to a mechanism of the reduction of NO 3 − . Copyright © 2004 John Wiley & Sons, Ltd.
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