Molecular understanding of heteronuclear active sites in heme–copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling

Abstract

Review surveying biomimetic modeling and molecular understanding of heteronuclear metalloenzyme active sites involved in dioxygen, nitric oxide, and sulfite reduction.

Shaping the Electrocatalytic Performance of Metal Complexes for CO2 Reduction

“…This being so, primarily because of their involvement in natural systems performing such processes. Metalloporphyrin‐containing enzymes are for instance implicated in the reduction of oxygen, nitrite, sulfite, and the reductive activation of oxygen, among others [4–7] . Although metalloporphyrins are not involved at the catalytic sites of the key enzymes that fix CO 2 in nature, [8] chemists have been interested in examining their potentialities for this particular task.…”

Cross‐talk Between (Hydrogen)Sulfite and Metalloproteins: Impact on Human Health

“…The reduction of sulfite to sulfide is a vital step in the biogeochemical sulfur cycle, which is driven by a class of metalloenzyme, namely sulfite reductase (SiR) [145–148] . These enzymes are widespread in bacteria, plants and fungi.…”

Nickel-mediated N–N bond formation and N2O liberation via nitrogen oxyanion reduction

“…[10][11][12] Soluble nitrate is abundant in runoff from agricultural elds, and accumulates in poorly ushed rivers, bays and seacoasts which ultimately leads to eutrophication and oxygen-poor "dead zones." [13][14][15] The reduction of nitrogen oxidation states is biologically accomplished by a variety of enzymes [16][17][18][19][20][21][22][23] and its synthetic conversion is essential to repurpose environmental pollutants into value-added compounds that might be derived from nitrogen oxyanions. An attractive route to nitrogen oxyanion reduction is through deoxygenation, [24][25][26][27][28][29][30][31][32] and the oxygen can be captured by protons, metal electrophiles, or main group elements known for their oxophilicity.…”