Experimental Determination of an Isolated trans-Dinitrosyl Manganese(II) Heme Analogue

Angew Chem Int Ed Engl. 2023 Apr 11;62(16):e202217545. doi: 10.1002/anie.202217545. Epub 2023 Mar 6.

Abstract

The lack of direct proof in either natural or synthetic systems for trans-dinitrosyl hemes, a key intermediate in the reactions of heme proteins (e.g. soluble guanylate cyclase (sGC), cytochrome c' and So H-NOX) with nitric oxide (NO), has hampered understanding of the exact reaction mechanisms, such as the formation of the five-coordinate heme complex with NO at the proximal side (5c NOP ). Herein, we report the first isolation of a dinitrosyl metalloporphyrin complex, the six-coordinate, low-spin {Mn(NO)2 }7 species [Mn(TPP)(NO)2 ] (TPP2- =meso-tetraphenylporphyrin dianion). The complex shows distinct features, such as an elongated axial bond (1.877(9) vs. 1.641(5) Å), a higher NO stretching bond position (1760 vs. 1735 cm-1 ) and an isotropic resonance at g = 2.0, in sharp contrast to those of five-coordinate mononitrosyl analogues. In situ diffuse reflectance infrared Fourier transform spectroscopy (DRIFT) and EPR studies provided deep insight into the reaction processes, demonstrating different responses of porphyrinates to NO.

Keywords: Crystal Structure; Electronic Structure; Manganese; Nitrosyl Ligands; Porphyrins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Guanylate Cyclase* / chemistry
  • Guanylate Cyclase* / metabolism
  • Heme / chemistry
  • Hemeproteins* / metabolism
  • Manganese
  • Nitric Oxide / chemistry

Substances

  • Guanylate Cyclase
  • Manganese
  • Heme
  • Hemeproteins
  • Nitric Oxide