Reduction of N2 by supported tungsten clusters gives a model of the process by nitrogenase.

Scientific Reports
Junichi Murakami, Wataru Yamaguchi

Abstract

Metalloenzymes catalyze difficult chemical reactions under mild conditions. Mimicking their functions is a challenging task and it has been investigated using homogeneous systems containing metal complexes. The nitrogenase that converts N(2) to NH(3) under mild conditions is one of such enzymes. Efforts to realize the biological function have continued for more than four decades, which has resulted in several reports of reduction of N(2), ligated to metal complexes in solutions, to NH(3) by protonation under mild conditions. Here, we show that seemingly distinct supported small tungsten clusters in a dry environment reduce N(2) under mild conditions like the nitrogenase. N(2) is reduced to NH(3) via N(2)H(4) by addition of neutral H atoms, which agrees with the mechanism recently proposed for the N(2) reduction on the active site of nitrogenase. The process on the supported clusters gives a model of the biological N(2) reduction.

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Citations

Aug 9, 2017·Physical Chemistry Chemical Physics : PCCP·Tao LiuStephen J Jenkins
Nov 16, 2017·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Heejune Park, Giovanni Meloni
Jan 29, 2014·Chemical Reviews·Brian M HoffmanLance C Seefeldt
Sep 16, 2017·The Journal of Physical Chemistry. B·Miguel A NiñoJuan M Rojo

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Methods Mentioned

BETA
X-ray
thermal desorption spectroscopy
thermal

Software Mentioned

XPSPEAK

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