Reactions of HNO with heme proteins: new routes to HNO-heme complexes and insight into physiological effects.
The formation and interconversion of nitrogen oxides has been of interest in numerous contexts for decades. Early studies focused on gas-phase reactions, particularly with regard to industrial and atmospheric environments, and on nitrogen fixation. Additionally, investigation of the coordination chemistry of nitric oxide (NO) with hemoglobin dates back nearly a century. With the discovery in the early 1980s that NO is biosynthesized as a molecular signaling agent, the literature has been focused on the biological effects of nitrogen oxides, but the original concerns remain relevant. For instance, hemoglobin has long been known to react with nitrite, but this reductase activity has recently been considered to be important to produce NO under hypoxic conditions. The association of nitrosyl hydride (HNO; also commonly referred to as nitroxyl) with heme proteins can also produce NO by reductive nitrosylation. Furthermore, HNO is considered to be an intermediate in bacterial denitrification, but conclusive identification has been elusive. The authors of this article have approached the bioinorganic chemistry of HNO from different perspectives, which have converged because heme proteins are important biological targets of HNO.
Kumar
Murugaeson R
MR
Department of Chemistry and Biochemistry, Baylor University, Waco, Texas 76706, USA.
Fukuto
Jon M
JM
Miranda
Katrina M
KM
Farmer
Patrick J
PJ
D000818:Animals; D006420:Hemeproteins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009603:Nitroso Compounds / Q000737:chemistry* / Q000378:metabolism
D006420:Hemeproteins; D009603:Nitroso Compounds