Why do nitrogenases waste electrons by evolving dihydrogen?

Seiji Ogo, Bunsho Kure, Hidetaka Nakai, Yoshihito Watanabe, Shunichi Fukuzumi

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

In nature, nitrogen is commonly fixed as the most reduced form, ammonia (NH3) and as the most oxidized form, i.e. nitrate ion (NO 3-). Nitrogenases catalyze the reduction of N2 into NH3 by using protons and electrons with evolution of H 2. However, the reason why the enzymes waste electrons by evolving H2 has yet to be clarified. We have previously reported (J. Am. Chem. Soc. 2002; 124: 597) pH-dependent heterolytic cleavage of H2 and subsequent reduction of NO3- with evolution of H 2 by iridium complexes in water. We propose herein a catalytic mechanism of nitrogenases, which can account for evolution of H2 in the reduction of N2 to NH3 in relation to a mechanism of the reduction of NO3-.

Original languageEnglish
Pages (from-to)589-594
Number of pages6
JournalApplied Organometallic Chemistry
Volume18
Issue number11
DOIs
Publication statusPublished - Nov 1 2004
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Inorganic Chemistry

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