Two CO molecules can bind concomitantly at the diiron site of NO reductase from Bacillus azotoformans

Shen Lu, Suharti, Simon De Vries, Pierre Moenne-Loccoz

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Abstract

CO complexes formed in reduced nitric oxide reductase from Bacillus azotoformans were investigated with resonance Raman and FTIR techniques. These experiments shows the presence of two ν(C-O) bands, one at 1970 cm-1 assigned to the heme-CO complex, and one at 2070 cm-1 from the non-heme iron, FeBCO. At cryogenic temperatures, the heme-CO complex adopts a semi-bridging configuration with FeB which decreases its stretching frequency to 1910 cm-1 and decreases the ν(C-O) of FeBCO by 20 cm-1. The concomitant binding of two CO molecules, one per iron(II) at the active site, is consistent with the formation of a [{FeNO}7]2 iron-nitrosyl dimer during substrate turnover. This study strongly supports the notion that this family of enzymes utilizes a reaction mechanism based on catalysis by proximity, where the formation of two iron-nitrosyl groups promotes N-N bond formation.

Original languageEnglish (US)
Pages (from-to)15332-15333
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number47
StatePublished - Dec 1 2004

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Bacilli
Carbon Monoxide
Bacillus
Oxidoreductases
Iron
Molecules
Heme
Nitric oxide
Fourier Transform Infrared Spectroscopy
Catalysis
Catalyst supports
Dimers
Cryogenics
Stretching
Catalytic Domain
Enzymes
Temperature
Substrates
Experiments
dinitrosyl iron complex

ASJC Scopus subject areas

  • Chemistry(all)

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Two CO molecules can bind concomitantly at the diiron site of NO reductase from Bacillus azotoformans. / Lu, Shen; Suharti; De Vries, Simon; Moenne-Loccoz, Pierre.

In: Journal of the American Chemical Society, Vol. 126, No. 47, 01.12.2004, p. 15332-15333.

Research output: Contribution to journalArticle

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AB - CO complexes formed in reduced nitric oxide reductase from Bacillus azotoformans were investigated with resonance Raman and FTIR techniques. These experiments shows the presence of two ν(C-O) bands, one at ∼1970 cm-1 assigned to the heme-CO complex, and one at ∼2070 cm-1 from the non-heme iron, FeBCO. At cryogenic temperatures, the heme-CO complex adopts a semi-bridging configuration with FeB which decreases its stretching frequency to ∼1910 cm-1 and decreases the ν(C-O) of FeBCO by ∼20 cm-1. The concomitant binding of two CO molecules, one per iron(II) at the active site, is consistent with the formation of a [{FeNO}7]2 iron-nitrosyl dimer during substrate turnover. This study strongly supports the notion that this family of enzymes utilizes a reaction mechanism based on catalysis by proximity, where the formation of two iron-nitrosyl groups promotes N-N bond formation.

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