Heme/non-heme diiron(II) complexes and O2, CO, and NO adducts as reduced and substrate-bound models for the active site of bacterial nitric oxide reductase

Ian M. Wasser, Hong Wei Huang, Pierre Moënne-Loccoz, Kenneth D. Karlin

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60 Scopus citations

Abstract

As a first generation model for the reactive reduced active-site form of bacterial nitric oxide reductase, a heme/non-heme diiron(II) complex [( 6L)FeII-FeII-(CI)]+ (2) {where 6L = partially fluorinated tetraphenylporphyrin with a tethered tetradentate TMPA chelate; TMPA = tris(2-pyridyl)amine} was generated by reduction of the corresponding μ-oxo diferric compound [(6L) FeIII-O-FeIII-CI]+ (1). Coordination chemistry models for reactions of reduced NOR with O2, CO, and NO were also developed. With O2 and CO, adducts are formed, [(6L) FeIII(O2-)(thf)⋯FeII-Cl] B(C6F5)4 (2a·O2) {λmax 418 (Soret), 536 nm; νO-O = 1176 cm -1, νFe-O = 574 cm-1 and [( 6L)FeII(CO)(thf)FeII-Cl]B(C6F 5)4 (2a·CO) {νCO 1969 cm -1}, respectively. Reaction of purified nitric oxide with 2 leads to the dinitrosyl complex [(6L)Fe(NO)Fe(NO)-Cl]B(C6F 5)4 (2a·(NO)2) with νNO absorptions at 1798 cm-1 (non-heme Fe-NO) and 1689 cm-1 (heme-NO).

Original languageEnglish (US)
Pages (from-to)3310-3320
Number of pages11
JournalJournal of the American Chemical Society
Volume127
Issue number10
DOIs
StatePublished - Mar 16 2005

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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